Final Exam (cumulative) Flashcards

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1
Q

definition of a cell

A

smallest functional unit of an organism

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2
Q

cell appendages

A

microvilli: finger-like projections from cell surface, non-motile. increase surface area
primary cilium: non-motile, sensory function, ubiquitous
motile cilia: hair-like structures filled with microtubules, beat in unison and move mucus layer
flagella: long, whip-like structure found only in sperm, used for swimming

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3
Q

endosymbiotic theory

A

mitochondria and chloroplasts are descendants of previously free living prokaryotic cells. theory created by Lynn Margulis

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4
Q

plasma membrane structure

A

two leaflets oriented with tails together in middle. PS and PE inside leaflet, PC and sphingomyelin outside.

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5
Q

lipid rafts

A

areas of membrane with longer tailed FA and cholesterol and sphingolipids, allows for more transmembrane proteins and are membrane hotspots for transmission

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6
Q

how do alpha helices form in transmembrane proteins?

A

must by about 20-30 amino acids in length and consist primarily of amino acids having non-polar or hydrophobic side-chains

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7
Q

types of membrane proteins

A
Integral Transmembrane:
single pass transmembrane
multipass transmembrane
beta-barrel transmembrane
Integral Monotopic:
hydrophobic alpha helix face inserts into one monolayer
Anchored:
lipid or GPI anchored into membrane
Peripheral:
associate with membranes non-covalently through integral proteins
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8
Q

topological equivalence

A

areas of the cell that have the same environment and are equivalent. includes the ER, Golgi, vesicles, and extracellular space

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9
Q

what determines permeability of a lipid bilayer?

A
molecular size
electrical charge
lipid-solubility
hydrophobicity
most soluble molecules are small, uncharged, hydrophobic, and lipid soluble
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10
Q

types of transport

A

passive: solutes move along gradient, no energy required
primary active: solutes move against gradient, direct energy requirement ((pumps))
secondary active: solutes move against gradient, uses favorable concentration gradient to move
symporter: coupled secondary active that moves both solutes in same direction
antiporter: coupled secondary active that moves solutes in opposite directions

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11
Q

how do pumps differ from coupled transporters?

A

pumps are enzymes, usually ATPases, that mediate primary active transport
coupled transport proteins are not enzymes, they are toggle proteins, that mediate secondary active transport

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12
Q

what is the resting membrane potential of a cell? how is it created?

A

RMP is the difference in electrical potential across the plasma membrane, magnitude is between -20 mV and -100 mV
created by K+ ions diffusing in both directions and having a higher concentration inside the cell

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13
Q

nodes of ranvier

A

VGNCs are only present at nodes of ranvier, so action potentials only occur at the nodes. results in saltatory (jumping) conduction which is much faster conduction

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14
Q

steps in vesicular chemical synaptic transmission

A

presynaptic depolarization by AP causes Ca2+ influx through VGCCs. exocytosis of neurotransmitter-containing synaptic vesicles and binding of neurotransmitter to postsynaptic receptors. this changes postsynaptic membrane conductance/potential, results in diffusion, degradation, and/or reuptake of neurotransmitter. synaptic vesicle membrane is retrieved and recycled

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15
Q

structure of nuclear envelope pores

A

big complexes that are selective (gated). channel nucleoporins act as size-selection filter, nuclear basket is located on nucleus side and cytosolic fibrils are on the cytosolic surface

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16
Q

steps in nuclear import

A

cargo with nuclear localization signal is recognized by nuclear import receptor and taken into nucleus. Ran-GTP binds and causes release of cargo and exits nucleus. Upon entering cytosol, Ran is hydrolyzed and Ran-GDP dissociates from receptor

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17
Q

steps in ribosomes docking to the ER

A

emerging protein has an ER signal sequence that an SRP binds to and halts translation. attached SRP binds SRP receptor in ER membrane and positions ribosome near protein translator channel complex which it docks with. once ribosome is docked, SRP and SRP receptor dissociate and translation continues feeding into ER

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18
Q

what does the seam in the translocator complex do?

A

allows for ejection of the protein at stop-transfer sequences via lateral gating. this creates transmembrane proteins

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19
Q

how are incompletely folded proteins prevented from leaving ER?

A

calnexin binds to unfolded proteins with terminal glucose residues and prevents them from leaving. glucosidase removes the glucose residues, but if protein fails to fold completely glucose residue is re-added by glucose transferase. cycle continues until folded correctly and no glucose residue is added, allowing protein to leave

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20
Q

how are phospholipids in membranes distributed appropriately? enzymes

A

ER scramblase: flips phospholipids from cytosolic to lumens leaflet
PM flippase: specifically flips PS and PE to cytosolic leaflet
PM scramblase: only active during cell death, events

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21
Q

types of coat proteins

A

clathrin: found in PM and trans-golgi
COPI: cis-golgi
COPII: ER
retromer: endosomes in retrieval pathway

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22
Q

steps in formation of vesicles (clathrin coated)

A

cargo receptors bind specific cargo and recruit to vesicle. adaptins bind cytosolic domains of cargo receptors and recruit clathrin. clathrin induces curvature and budding. the clathrin and adapting dissociate from vesicle after budding due to Rab hydrolyzing GTP.

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23
Q

what’s dynamin and what happens when it doesn’t work?

A

dynamin is a monomeric G protein that contracts the neck of budding vesicles and causes scission. Shibire mutants in drosophila had inhibited vesicle scission and recycling of exocytosed vesicles is greatly reduced, clathrin coated pits are long tubes and fly is paralyzed

24
Q

important subunits of retromer

A

BAR: mediates dimerization, attaches to curved bilayers only
PX: binds to PIP in membrane

25
Q

How does pH change in ER to golgi? why is this important for signaling?

A

pH decreases from neutral in the ER to acidic in the trans golgi. signals like KDEL are pH dependent because the KDEL receptor binds its signal at acidic pH but does not bind it at neutral pH, resulting in KDEL signal proteins being released only in the ER

26
Q

2 models of Golgi traffic

A

vesicular transport model: golgi stacks are static and vesicles move forward and backward
cisternal maturation model: golgi stacks migrate and mature, vesicles only move backwards

27
Q

how are hydrolases delivered to early endosomes/lysosomes?

A

hydrolases contain a M6P signal that is recognized in the golgi and bound by M6P receptors. these recruit in vesicles and transport to early endosome. hydrolases unbind from receptors due to more acidic pH in the early endosome

28
Q

difference between micropinocytosis and phagocytosis mechanisms?

A

micropinocytosis uses actin ruffles

phagocytosis uses actin pseudopods

29
Q

what are caveolar microdomains?

A

they are buds from lipid rafts, often targets of viruses and toxins. cholera toxin enters through caveolar microdomains and causes illness by increasing chloride production and causing massive movement of water

30
Q

general overview of pathway of endocytose material

A

endocytosed from PM, goes from early endosome to recycling endosome or multi vesicular body, then late endosome, then endolysosome, then finally lysosome

31
Q

what’s the point of multi vesicular bodies? how are they formed?

A

intralumenal vesicles allow for degradation of membrane proteins. receptors are tagged with ubiquitin to signal sequestration and degradation

32
Q

steps of vesicle fusion

A

first Rab (vesicle) and Rab effector (target) meet and tether. then docking can occur as vesicle gets closer to membrane. SNAREs can pair and Rab is released. t-SNAREs winch with v-SNAREs and bring bilayers within 2 nm, leading to fusion. SNAREs untwist for re-use

33
Q

what are GAPs and GEFs?

A

GTP binding proteins are regulated by GAPs and GEFs. GAP causes GTP hydrolysis which switches the protein off/inactive. GEF causes release of the GDP which allows GTP to bind, switching the protein on/active.

34
Q

GPCRs activate which subunit of heterotrimeric G proteins? what is a GPCR to a G protein?

A

activated GPCRs will activate the alpha subunit, causing the beta/gamma to dissociate and both subunits to activate. the GPCR switches the alpha to activate so functions as a GEF

35
Q

signal pathway to activate protein kinase C

A

signal molecule activates GPCR which activates G protein. IP3 is released and binds IP3 receptors on ER and allows calcium to exit. DAG and calcium activate protein kinase C which plays a role in signal transduction cascades

36
Q

what is calmodulin? how does it effect downstream proteins?

A

calmodulin (CaM) may bind downstream effector proteins only after being activated by Ca2+. Once activated, CaM can activate calmodulin kinase CaMK which phosphorylates proteins at serine/threonine residues

37
Q

pathway of Ras activation by RTK

A

signal activates RTK phosphotyrosines (SH2 domains) to bind Grb-2 adaptor protein, which also binds polyproline regions on Ras-GEF (SH3 domains). the Ras-GEF then induces Ras to become active.

38
Q

what does it mean that actin has polarity?

A

there is a plus and a minus end. the minus end has the ATP binding site and actin monomers are added to the plus end

39
Q

how do bacteria exploit actin polymerization?

A

assembly of actin on the bacterias surface propels the bacteria forward, helping them invade neighboring cells

40
Q

how does myosin “walk”?

A

myosin heads bind and hydrolyze ATP. head undergoes conformational changes that lead to walking of heads along actin filaments. when ATP bound head dissociates from actin and moves, when ADP bound it binds weakly in the new position, when ADP leaves it binds tightly and swings back so “walking” occurs.

41
Q

what causes a protofilament to be straight or curved?

A

when the tubulin dimer is GTP bound it is straight. after GTP hydrolysis to GDP, the filament is curved.

42
Q

what are gamma TuRCs?

A

nucleation sites for microtubules found on the centrosome. they have a ring structure that serves as a template for tubular microtubule formation

43
Q

how do kinesin and dynein differ?

A

kinesin walks toward the plus end while dyneins walk towards the minus end of microtubules. cargo can bind both types and coordinate movement either direction

44
Q

what are basal bodies? what arrangement do they promote?

A

basal bodies serve as the template for formation of microtubules to make the axoneme. one basal body is found at the base of a cilium or flagellum. there is a 9 + 2 arrangement of microtubules within flagellum and cilium

45
Q

what is myostatin? what does deficiency cause?

A

a growth factor that inhibits muscle cell growth. inactivating myostatin causes double-muscling where the organism has uncontrolled muscle growth.

46
Q

how is entry into the cell cycle controlled?

A

Cell cycle control system CCCS is a series of biochemical switches/checkpoints that control the cell cycle. signals cause response and allow cycle to proceed pass checkpoints.
Start transition
G2/M transition
Metaphase-to-anaphase transition

47
Q

Cdks

A

cyclin dependent kinase. evolutionarily conserved in all eukaryotic cells. specialized function as CCCS signals. Cdks are activated by cyclin at critical concentration, cyclin fluctuates through cell cycle to control Cdk activity and checkpoint passing

48
Q

telomeres

A

the ends of chromosomes consisting of TTAGGG repeats. end replication problem means that chromosomes become shorter with each replication event. critically short telomeres activate DNA damage response and trigger arrest of cell cycle

49
Q

HeLa Cells (immortalized cell lines)

A

immortalized cell lines can divide indefinitely and provide genetically identical cells. most used cell line is HeLa Cells from Henrietta Lacks cervical cancer cells

50
Q

how is apoptosis caused by internal signals?

A

cytochrome c is released from mitochondria and promotes assembly of Apoptosome. this then activates caspase cascade via procaspases (initiator caspases)

51
Q

how is apoptosis caused by external signals?

A

Fas ligand (on killer lymphocyte) binds to Fas death receptors on cell and triggers activation of caspase cascade (dimerization) and apoptosis

52
Q

what regulates intrinsic apoptosis pathway?

A

Bcl2 protein family. includes Bak and Bax as pro-apoptotic triggers that release cytochrome c. Bcl2 and BclX are anti-apoptotic and block cytochrome c release

53
Q

Satellite cells

A

Stem cells that are inactive and lie near mature muscle cells. Once activated, satellite cells proliferate and fuse with muscle to repair damage

54
Q

How is the vascular system remodeled?

A

Endothelial cells can be used to create capillary sprouts in response to VEGF, which is a growth and survival factor

55
Q

Red blood cells

A

Cannot grow or divide. Erythropoietin is necessary for survival of RBC progenitors.

56
Q

Platelets

A

Considered mini cells. They bud off and are very small cells used to help with repairs and clotting

57
Q

Transdifferentiation vs iPS

A

iPS involves deprogramming a cell back to a stem cell and then reprogramming it to a different type. Transdifferentiation goes straggly from one cell type to another without going back to stem cell.