Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

MCM comp > Exam I > Flashcards

Exam I Flashcards

1
Q

Viruses store DNA in what form

A

RNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

why is it called “deoxy” ribose in DNA

A

no OH on the 2’ carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

3 parts of a nucleotide

A

deoxy or oxy ribose sugar, 1 phosphate group, and nitrogenous base (ATCG)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

backbone linkage on DNA

A

covalent phosphodiester bonds, between triphosphate and the 3’carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what direction does DNA pol read and write strands

A

reads 3’–> 5’ synthesizes 5’–>3’

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

direction of exonuclease activity, why?

A

3’–>5’ because if we cut from 5’ end we lose triphosphate..which we need to grow the strand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

RNAse H

A

chews out single ribonuscleoside in between okazaki fragments

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

ssbinding poteins

A

keep DNA that has just been unzipped to stay apart

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

enzymes req what to get DNA pol at every primer

A

multi enzyme complex, DNA helices, clamp and clamp loader, DNA polymerase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

DNA origin of replication usually have what sequence and proteins?

A

AT rich because these only have 2 H bonds

proteins are bound here: cycline dependent kinases, loads DNA helicase nearby

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How many rep forks are made in DNA

A

2, replication bubble

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

When does DNA synthesis occur in cell cycle

A

S phase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

chromatin

A

nuclear DNA with proteins assoc with it. lots and lots of protein. beads on a string. histones and non histonal chromosomal proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

nucelosome

A

DNA wrapped in proteins and histones. Protein core with 8 different histones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

fifth histone protein H1

A

located outside of nucleosome and holds it together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

histone tails

A

lysine and arginine (+) charges to interact with DNA(-)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

2 types of chromatin

A

10nm fiber and

30nm fiber from H1 interaction–>makes it a condensed structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Want to transcribe DNA sequence, how do we unravel it from 30nm fiber form?

A

acetylation that will cause binding to the lysine and argentine bases so we can access the DNA. prevent 30nm fiber from forming

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

chromosomes

A

condense chromatins into chromosomes using non histone proteins.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

epigenetic inheritance in DNA synthesis

A

50% parents histones(methylated) are passed down to daughter cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

termination of synthesis on lagging strand

A

use telomerase, which using reverse transcriptase(RNA template to make DNA)
short tandem sequence added. elongates 5’–>3’ of parental strand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

overhang from telomerase activity

A

“tucked in” to prevent form degradation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Central dogma

A

DNA–>RNA–>proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

gene expression

A

DNA synthesis, transcription and translation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

differences in RNA and DNA

A

RNA: Uracil, extra OH on 2’, single stranded

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

RNA polymerase II is able to do what with no help

A

can bind, begin without primer and make many mistakes–> not as big of a deal because transcripts can be degraded.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

RNA pol 1, 2 ,3

A

RNA pol I–> rRNA synthesis: makes proteins
RNA pol II–> mRNA: protein coding genes, siRNA miRNA: silencing
RNA po lII–> tRNA, rRNA, snRNA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What does RNA pol II need

A

General Transcription factor: TFIID, recognizes TATA box, AT rich sequence. This is before promoter and causes aggregation of more transcription factors that will help to open DNA and begin transcription

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

CTD tail

A

On C terminal domain of RNA pol II, going to be phosphorylated, functions to make changes to emerging mRNA molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

mRNA is transcribed where

A

in nucleus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What needs to happen to move mRNA out of nucleus

A

1: methylated GMP cap at 5’ because this emerges first(5’–>3’)
2: splicing of introns- snRNPs
3: Poly A tail at 3’

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Sites for splicing

A

edges and intersections of exons/introns

5’ site, branch point, 3’ site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

ribonucleotide protein hnRNPs

A

ribose sugar with nucleotide with a protein

so it can complementary base pair with NT

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

Poly A tail initiation

A

sequence coding for termination, causing cleavage, Poly A polymerases add tons of As
requiring a lot a lot of energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

rRNA

A

80%. Pol I No CTD tail, no capping no Poly A tail
many subunits come together to make this molecule
snoRNAs help to post transcriptionally modify rRNA
small and large subunits assembled outside before brought back in

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

most genes encode for what

A

mRNA–> proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

charged tRNA

A

carries aa, and anticodon that codes for that aa its carrying

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

wobble position

A

3rd nucleotide space of codon has some variability and still codes for same aa– Silence mutation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

2 important areas in tRNA

A

charged aa at 3’ end

read transcript 5’–>3’ so the anticodon loop is read 3’–>5’

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

amino acyl tRNAse

A

add aa to tRNA using ATP 3’ OH group on NT interacts with OH on aa
aa on C terminus carries activation energy to link next aa

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

direction of protein synthesis

A

begins N terminus–> C terminus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

subunits of rRNA

A

small is responsible for recognition of codon

large: addition of peptide bond, adding aa to protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

4 sites of ribosome

A

mRNA binding site, A(arrival) site, P(peptide), E(exit

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

where is peptide synthesis in rRNA

A

A site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

how do tRNA get to A site

A

chaperones, elongation factors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

ribozyme

A

ribosomal molecule that catalyzes a reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Initiation peptide synthesis

A

Start codon: AUG -methionine met-tRNAi
met usually removed afterwards
binds into P site in small subunit when finds AUG
(initiation factors leave at this point)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Termination of translation

A

Stop: UGA UAA UAG
molecular mimicry- don’t code for aa
bind in A site and peptidyl transferases add a OH to C terminus to release peptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

Protein structure vs function

A

structure equals function!

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Structures of Proteins

A

primary: aa sequence
secondary: alpha helices and beta sheets: covalent bonds
tertiary: final form of protein
quaternary: multiple tertiary structures

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Molten globules state

A

secondary structure needing chaperones to shift into tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

Protein folding chaperones

A

Help with correct confirmation, usually assoc with ribosome. Heat shock proteins (inc heat= incorrect folding so inc production of these proteins)
look for hydrophobic patches on exterior, should be on interior.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Hsp70

A

bind protein as emerging from ribosome if locate hydrophobic patches

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Hsp60

A

forms a barrel or protective environment for correct protein folding (molten globule states)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

if protein is incorrectly folded

A

no functioning properly usually degraded by proteasome that has a cap to recognize protein (poly ubiquital chain)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

Ubiquitin cascade

A

E1 activate ubiquitin, activates E2 by transferring the ubiquitin to it then this takes it to target. E3 recognizes which protein needs to be degraded.
E3 has E2 attached and adds ubiquitin to lysine side chain to make ubiquitin tag

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

E3 activation/inhibition

A

ligand, another subunit, also can unmask degradation signals(removing subunit), cause destabilizing N terminus(removing 12 aa sequence)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

cytoskeleton units

A

microtubules, intermediate filaments, microfilaments

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

microtubules

A

dimers of alpha and beta subunits. oligomers of dimers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

protofilaments

A

huge chains of oligomers, form in sheets–>tubulin sheet which roles and folds into a tube
grow at one end via adding dimers, degrade at another

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

2 groups of microtubules

A

stable: permanent like cilia and flagella. don’t degrade very quickly
centrioles or MTOC are stable as well
dynamic: the mitotic spindles. come and go, always in flux.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

structure of stable microtubule

A

ex cilium: 9+2 with dynein arms and in middle are two microtubules. Covered by cell membrane (bilaminar phospholipid)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

centriole structure

A

basal body is anchoring structure. 9 triplet structure: more stable
g-tubulin proteins to help integrate cilia into basal body

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

cilia

A

move stuff, line epithelia tract.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

centrosomal area components

A

pericentriolar mass and centriole

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
66
Q

dynamic microtubules are found

A

cytoplasm, pave roads for like dynein motor proteins and kinesin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
67
Q

kinesin

A

brings structures to where they need to go in the cell. like vesicles or NT

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
68
Q

microfilaments

A

actin or myosin(muscle) 5-8 nm

surround nucleus

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
69
Q

actin

A

cell contraction! and locomotive processes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
70
Q

tropomodulin structural protein

A

caps actin so can’t grow

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
71
Q

cofilin

A

severs actin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
72
Q

filamin

A

cross links actin filaments–>gelatinous structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
73
Q

tropomysin

A

stabilizes actin filament–>skel m contraction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
74
Q

Intermediate filaments

A

6 classes of IFs very specific

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
75
Q

Type I and II IFs

A

keratins and prokeratins
epithelial cells
specific keratin can be associated with cancers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
76
Q

Type III IFs

A

desmin, found in all mm cells.
vimentin, found in non muscle cells-mesoderm derived
glial fibrillary: astrocytes, stabilize neurons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
77
Q

Type IV IFs

A

neurofilaments. found in neurons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
78
Q

Type V IFs

A

lamins–> structure to nucleus and help form nuclear pore(transcription regulation)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
79
Q

Type VI IFs

A

developmental. ex nestin, usually found in islet beta cells to indicate formation of beta cells, then disappear.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
80
Q

blistering, whats going on inside

A

separation of epithelia cells in skin= fills with fluid

irritation caused

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
81
Q

Ritters disease

A

neonatorum. Staph aureus infection of skin. exotoxin is released from this bacteria. Exotoxin attaches and binds to desmosome and denatures them so epithelial cells lose adhesion to one another.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
82
Q

2 phases cell cycle general

A

Interphase:G1-2n (G0) S-4n and G2-4n

M phase: mitosis: prophase metaphase anaphase telophase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
83
Q

homologues

A

not connected to each other. diploid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
84
Q

signals for cell to go back into G1 from Go

A

growth factors or mitogens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
85
Q

restriction point of cell cycle

A

G1–>S go into Go

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
86
Q

G2/M chkpoint

A

chrom alignment at metaphase, need to know that DNA replicated and environment is good

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
87
Q

met/anaphase chkpoint

A

sisterchromatids and spindles formed correctly

88
Q

Cdks

A

phosphorylate proteins that regulate cell cycle

89
Q

cyclins

A

bind to Cdks to activate them. Undergo cell cycle dependent production

90
Q

cyclin Cdk

A

particular kinase. cdk activating kinase

91
Q

wee1

A

phosphorylation to inhibit Cdk

use cdc25 to remove inhibitory phosphate

92
Q

Cdk inhibitor proteins

A

bind the complex and inhibit activity

p27, 21 16

93
Q

E3 ligases in cell cycle

A

anaphase promoting complex APC, activated by cdc20

94
Q

G1 main events

A

pre replicative complex

add DNA helicase, assemble proteins and activate S Cdk by producing S cyclin

95
Q

S phase main events

A

S-Cdk, centrosome duplicated(semiconservative), cohesins, pre-initiation complexes
DNA synthesis

96
Q

G2 main events

A

M cyclin –>MCdk CAKinase Pi site or Wee1 inhibits site, so cdc25 can dephos wee1
and condensin gets Pi to condense sister chromatids.

97
Q

(+) ends in spindles

A

growing out! towards sister chromatids

98
Q

dyneins move what direction

A

towards (-) so towards centrosome

99
Q

APC/C in M phase

A

ubiquitilating proteins that need to be degraded.
like securin, to activate separase so sister chromatids can split.
also leads to ubiquitlation of MCdk so cell cycle can terminate

100
Q

Cytokinesis

A

cleavage furrow–> uses actin because contractile ring
activated through RhoA-GTPase. inactive-GDP Guanine exchange factor-GEF switches out for GTP. leads to myosin light chain contraction= actin contraction

101
Q

basic dyes

acidic dyes

A 
hematoxylin, toluidine blue, methylene blue
all stain (-) structures like DNA, RNA etc
eosin, acid fuschin--> basic structures some basic proteins
102
Q

osmolality

A

total concentration of particles in a container

water will flow where high [ ] are

103
Q

electroneutrality

A

charges in every compartment in cells wants to have equal + and - charges

104
Q

negative charge in cells is caused by

A

impermeable proteins

105
Q

simple diffusion

A

movement of small particles across the membrane that don’t need help. H2O, steroids, gases
[ ] dependent only

106
Q

facilitate diffusion

A

need protein to move it. carriers can become saturated

107
Q

flux is controlled by

A

distance need to move, diffusion properties and electrochemical gradients

108
Q

passive movement of H2O

A

osmosis: hydrostatic P used to move water, always maintain near 0 in cells
osmotic pressure: caused by osmolality like in capillaries

109
Q

aquaporins

A

little channels for H2O movement and sometimes glycerol and never charged particles
They are in every PM.

110
Q

what side of a cell is Na+ and Cl- high on

A

extracellular

111
Q

[ ] gradients can be used for what

A

transporting other solutes against their [ ] gradient

112
Q

Na+/K+ gate

A

inside of cell, 3 Na+ bind. phosphorylate channel which conformationally changes channel and lets Na+ out into extra cell. 2K+ bind causing conformational change so K+ released into cell

113
Q

Where is Ca2+ low

A

Cytosol. Ca2+ stored in extracellular stores because passively wants to move into cells! used for many pathways

114
Q

Proton [ ] gradient

A

wants to move into cells

115
Q

Cl- moves with

A

HCO3-. bicarb buffer system Cl- tries to balance out extreme + charge on extracellular side

116
Q

membrane potential

A

separation of charges across a membrane

117
Q

Inhibiting Na+/K+ pump causes?

A

Cell is going to swell because accumulation ions in cell

118
Q

hypertonic.hypotonic environments

A

hypertonic external: cell shrinks because water leaves

hypotonic external: cell swells because water comes in

119
Q

Cell response to acute cell shrinkage

A

activation of Na+/H+ exchanger. takes in Na+ extrude H+, the extrusion of H+ is going to activate the HCO3-/Cl- pump because cell is getting too basic. Net uptake NA+ and Cl- so increase [ ] so water will follow

120
Q

Cell response to acute cell swelling (too high [ ])

A

open K+ and Cl- channels, diffuse out via [ ] gradient

121
Q

long term changes in solute [ ] (dehydration or drinking too much H2O)

A

creates ideogenic osmolytes in the cell in response to shrinking because need to bring H2O in

122
Q

cytoplasmic pH

A

7.0-7.3

123
Q

Intracellular metabolic acidosis/alkalosis

A

acidosis low pH(move H+ out) alkalosis high pH (inhibit moving H+ out and start to pump HCO3- out)

124
Q

Intracellular respiratory acidosis

A

increase CO2 in blood will be driven into cell which produces carbonic acid and H+ and OH- ions. so drop pH because [H+] increased
Na/H exchanger to raise pH then when reached pH it inhibits itself
Cl-HCO3- exchanger lowers pH and when reached pH it inhibits itself

125
Q

Intrinsic buffers

A

Intracellular, cannot escape cells. so like charged residues on proteins that can donate H+

126
Q

how to proteins get to where they need to be?

A

sorting signals, found within the aa sequence
sorting patches
detected by charge

127
Q

describe the various types of protein transport

A

gated: selective (nuclear pore) topologically equivalent
transmembrane: protein has to transport across membrane: topologically distinct
vesicular: using budding then fusion

128
Q

signal sequences

A

N terminus 15-60 bases long. Usually cleaved after sorted

129
Q

signal patch

A

1 sequence or different parts of a protein that come together in 3D form

130
Q

direction of proteins in nucleus

A

proteins in, for transcription

mRNA out

131
Q

Nuclear pore

A

nuclear porins that form an octagonal ring with cytosolic fibers to direct molecules in, and a basket at other end
small molecules freely diffuse
proteins need assistance by chaperones

132
Q

nuclear localization signal

A

proteins sequence to be directed into nuc pore, arginine and lysine because (+) charges. charges interact with cytosolic fibrils

133
Q

nuclear import R

A

2 binding sites specialized for cargo proteins,1: nuclear localization signal and 2: FG repeats that allow Receptor to bind and move through pore

134
Q

nuclear import adaptor

A

in between nuclear import R and cargo protein

135
Q

mitochondrial proteins

A

synthesized in cytosol.

136
Q

HSP70s role in mitochondrial proteins

A

keep protein unfolded until transported into mitochondrial. has an N terminal sequence alpha helix-ampipathic, recognized by mitochondrial membrane Receptors

137
Q

Intermembrane mitochondrial proteins

A

N terminal seq directs to mito,

Internal sequence is a seq to insert protein into membrane. Need stop transfer sequence

138
Q

Stop transfer sequences

A

hydrophobic because destined to the membrane

139
Q

rER responsible for

A

beginning of protein trafficking. same as free ribosomes, but the sequence on protein is making ribosome translocate to rER

140
Q

cotranslational import

A

as protein emerges from mRNA, the N terminus has signal to interact with R on rER to be inserted into lumen of rER

141
Q

sequence on N terminus for rER insertion

A

signal recognition particle(srp) will bind N term sequence and pause translation so it can insert N term into membrane of rER via Signal recognition particle Receptor. srpR

142
Q

ER resident protein

A

have C terminal signal to keep them in ER “KDEL”

143
Q

protein glycosylation

A

happens in ER, tells protein to be in extracell membrane or cytosol. Blood types vary because of glycosylation. enzymes build oligosaccarides but then different enzymes chop down these sugars
signal that protein is folded correctly

144
Q

responses to misfolded proteins

A

heat shock response and unfolded protein response which happens on ER: initiate signals to increase chaperone amount and mRNA splicing for chaperone production or can reduce translation to influence flow of misfolded proteins

145
Q

GPI anchor

A

attaches in ER, used for PM proteins

146
Q

Vesicular transport

A

exocytosis: from ER to golgi to lysosome or PM or endocytosis: from PM or extracellular components

147
Q

membrane markers

A

on transport vesicles that tell vesicle where to go. transport vesicles use cytoskeleton to travel

148
Q

Cathrin coated vesicles go/from where

A

from PM, clathrin triskelions

149
Q

COPI

A

from golgi

150
Q

COPII

A

bud form ER

151
Q

Golgi apparatus function

A

sorting station for final destination using coating vesicles. Incoming have signals that say where they need to go. Exit signals have COPII signal

152
Q

how to unfolded proteins not enter vesicles

A

chaperones in ER cover the exit signals

153
Q

homotypic fusion

A

fusion of vesicles from same compartment
require t snares and v snares
example: vesicular tubular clusters

154
Q

heterotypic fusion

A

fusion of 2 vesicles from different compartments

155
Q

ER retrieval signals

A

C terminal lysine for KDEL sequence, bind COPI or KDEL R and returned to ER from golgi

156
Q

Golgi sides

A

Cis golgi is the entry side, trans is the exit side. median in the middle

157
Q

lysosomes

A

degradation. filled with acid hydrolyses- hydrolytic enzymes that require proteolytic cleavage to be active because its so destructive
pH 4.5-5.0

158
Q

how do we get low pH in lysosome

A

pump H+ via vacuolar H+ ATPase. uses ATP

159
Q

zymogen

A

enzyme that needs proteolytic cleavage to be activated

160
Q

early endosome

A

intially endocytosed molecules that contact with lysosomal hydrolyses, some can be recycled back to membrane

161
Q

late endosomes

A

mildly acidic interior, hydrolytic digestion begins, enzymes not completely active yet

162
Q

endolysosome

A

fusiong of late endosome and existing lysosomes, decrease pH to the 4.5-5.0 range

163
Q

autophagy

A

enclosure of organelle with autophagosome to fuse with lysosome and digest the organelles

164
Q

how do we get proteins to lysosome

A

Mannose residue attached to protein in ER, moved into golgi and enzymatic processes make it Mannose 6P
this signal packages in clathrin to go to lysosome

165
Q

melanocytes

A

specialized lysosomes will store melanin. the exocytosis of lysosomes bring melanin to surface
keratinocytes will endocytose pigment

166
Q

types of endocytosis

A

phagocytosis: large molecules in large vesicles called phagosomes
pinocytosis: fluid and small molecules

167
Q

constitutive secretory pathway

A

exocytosis via exit trans golgi network and secreted into extra cell space, membrane proteins and lipids are added to PM

168
Q

Regulated Secretory Pathway example

A

NT that signal release of ions. specialized cells that secrete hormone, enzymes etc.

169
Q

majority communication in cells

A

extracellular, cell signals, ligands, Receptors all that fun stuff

170
Q

cell differentiation

A

signals that can change the way a cell is forming so it becomes specific. these signals can be combinations

171
Q

Cells have same R in different tissues, how can the result be different?

A

intracellular cascade is specific to each cell type

172
Q

trophic factors

A

factors that are required for a cell to survive, without these cell undergoes apoptosis

173
Q

morphogen gradients

A

important in development, where a cell lies on gradient determines how the cell response
requires signaling centers and responding centers on cell

174
Q

desensitization

A

prolonged stimulus, cell sequesters the Receptor–> either down regulate(lysosome) or recycle. Can innactivate R. Can inactivate intracellular cascade parts, or induce an inhibitor of the intracellular cascade

175
Q

mitogens

A

stimulate cell division acivate through restriction site in cell cycle

176
Q

growth factors

A

not only can stimulate growth but also dictate cellular growth

177
Q

extracellular signaling categories

A

direct: cell-cell or cell-extracell matrix, gap junctions
endocrine: distance
paracrine: nearby cells
autocrine: works on self
synaptic: in synapse

178
Q

cross talk

A

interaction of signaling pathways, pos or negative interaction.

179
Q

Steroids

A

activate intracell R because hydrophobic can cross cell membrane. made from cholesterol

180
Q

R for Steroids

A

Intracellular Nuclear R superfamily, dimerize upon ligand binding. this directly acts as a transcription factor

181
Q

NO

A

activates intracell R. very short half life. activates guanylyl cyclase to produce cGMP from GTP= relaxation smooth m

182
Q

Peptides

A

activate extracell R. have peptide hormones, Growth Factors and neuropeptides

183
Q

Neurotransmitters

A

small hydrophilic. released from presynaptic membrane to act on post synaptic cell(have R)
ligand gated ion channel or GPCR

184
Q

Eicosanoids

A

locally. bing cell surface R. clotting and inflammation. Cyclooxigenase I and II inhibited by NSAIDs

185
Q

Ion Channel couple R

A

ionotropic. rapid signaling with ligands NT. open or close channel, change ion permeability and Mpotential

186
Q

GPCR metabolic

A

ligand binding on extracell, intracell C term has G proteins(alpha, beta gamma) associated with it.
ligands: eicosanoids, NT, peptide hormones

187
Q

which cell R associated with special sense?

A

GPCR sight, smell and taste

188
Q

Resting state GPCR

A

no ligand, alpha G protein bound by GDP and betagamma complex assoc with membrane

189
Q

Active state GPCR

A

GDP exchanged to GTP (GEF) on alpha which dissociates subunits.

190
Q

Deactivation GPCR

A

GTPase activating protein, exchanges GTP for GDP

191
Q

G alpha proteins and what they do

A

G stimulatory (activates adenlyly cyclase)
Ginhibitory (inhibits adenlyly cyclase)
Gq activate PKC

192
Q

Enzyme coupled R

A

extracell binding, intracell catalytic domain.

193
Q

R Tyrosine Kinase

A

Enzyme coupled. ligands: GFs dimerize when ligand binds and cross phosphorylate each other
intracellular cascade induces kinases

194
Q

Tyrosine Kinase Assoc R

A

act through tyrosine kinases
ligands: cytokines, interleukins and integrins
binding of ligands induce dimerization

195
Q

cytokine R

A

subclass TK assoc R. JAK/STAT

196
Q

Protein tyrosine phosphotases

A

inhibits pathway by dephosphorylating

197
Q

R guanylyl cyclase

A

activates cGMP

198
Q

R serine/threonine Kinases

A

TGF beta ligand. form heterodimers when active, one chain phosphorylates the other.
Smad pathway

199
Q

Notch

A

requires downstream proteolysis. developmental!
cell-cell binding of delta to notch
ligand induces cleavage of cytosolic tail–>nucleus to induce transcription

200
Q

Frizzled

A

Wnt pathway, when activated can induce the release of Beta catenin(stops phosphorylation of betacatenin aka degradation) so it can go into nucleus to act as a transcription factor

201
Q

patched/smoothened

A

hedgehog ligand. activates patched to activate smoothened which will inhibit Phosphorylation of Ci so Ci can enter nucleus and induce transcription

202
Q

Death R

A

extrinsic apoptosis. ligands: cytokines, GFs, pathogen assoc molecular patterns
homotrimeric. when one ligand binds the subunits cluster of domains
adaptor proteins with death domains will activate caspases. (8and10)

203
Q

Integrins

A

At cell-matrix junction. associate with cytoskeleton interiorly and extra cell matrix exteriorly so when sense movement outside can cluster and autophosphorylate FAKs, Focal Adhesion Kinases
these Pi sites serve as binding for signaling proteins

204
Q

second messengers

A

small intracellular signaling molecules. generated very fast and move very fast

205
Q

cAMP

A

formed form ATP by adenlyly cyclase, degraded to aMP by cAMPphosphodiesterase
induces PKA which is a tetramer of 2 subunits which will phosphorylate targets

206
Q

cGMP

A

formed from GTP by guanlyly cyclase, degraded to GMP by cGMPphosphodiesterase
activates protein kinases and ion channels

207
Q

PIP2

A

inner leaflet of plasma membrane. we use as second messenger

phospholipase C induces cleavage of PIP2 to IP3 and diacylglycerol (DAG)

208
Q

IP3 activates ligand gated Ca2+ channels

A

activates ligand gated Ca2+ channels

209
Q

DAG

A

activates PKC

210
Q

PI3 kinase

A

works on PIP2 to convert into PIP3

211
Q

PIP3

A

activates AKT= protein survival and synthesis

212
Q

MAP kinase

A

GFs and mitogen activated. regulate cell growth and differentiation.
RAS activation–> RAS Raf Mek Erk

213
Q

JAK/STAT

A

cytokine R, TK assoc. JAK is a nonreceptor tyrosine kinase that phosphorylates STATs
STATs dimerize when Pi and translocate to nucleus to act as transcription factor

214
Q

TGFbeta/SMAD

A

serine/threonine kinases phosphorylate one another. SMAD translocates to nucleus and acts as transcription factor

215
Q

NF-kB

A

Receptor is the tumor necrosis factor R.
ligands: cytokines, GFs, TNF
NF-kB is usually bound by inhibitory protein
activation Pi inhibitory protein= ubiquitilation
NF-kB moves to nucleus to act as TF

216
Q

Rho

A

regulate cytoskeletal changes, like focal adhesions, filopodia etc.
Activated via integrins and GF receptors.
promotes actin polymerization and phosphorylation of myosin light chain= contraction

MCM comp (2 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions