Brainscape's Knowledge GenomeTM

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


See full index

Cell Biology > Final 2 > Flashcards

Final 2 Flashcards

You may prefer our related Brainscape-certified flashcards:
AP® Biology flashcards Biology 101 flashcards
1
Q

Where do proteins without a sorting signal end up?

A

Stay in cytosol

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

Gated transport of the nucleus through what?

A

Nuclear pore complexes

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

3 types of intracellular transport

A

Gated, transmembrane, vesicular

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

2 types of sorting signals

A

Signal sequences, signal patches

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

How long are sorting signals?

A

15-60 continuous residues

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

How are signal sequences removed from a protein?

A

Signal pepidases

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

Proteins that make up a NPC

A

Nucleoporins

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

About how many NPCs does a mammalian cell contain?

A

3000-4000

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

True or false: nuclear proteins can be transported through a pore complex while folded

A

True

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

Binding sites for nuclear import receptors

A

F-G repeats

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

Provides energy for concentration of particular proteins on one side of the nuclear envelope

A

Ran

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

What kind of molecule is Ran

A

GTPase

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

Triggers hydrolysis of ATP, converting Ran-GTP to Ran-GDP in the cytosol

A

GAP (GTPase-activating protein)

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

Promotes the exchange of GDP for GTP, converting Ran-GDP to Ran-GTP

A

GEF (Guanine exchange factor)

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

Ran-____ is primarily in the cytosol; Ran-____ is primarily inside the nucleus

A

GDP, GTP

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

Where are mitochondrial signal sequences?

A

Amino-terminus

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

Completes mitchondrial import by repeated cycles of ATP hydrolysis

A

HSP70

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

Helps insert membrane proteins into outer membrane

A

TOM (translocase of outer membrane)

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

Spans both mitochondrial membranes and mediates translocation of proteins in to the matrix space

A

TIm23

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

Mediates the insertion of a subclass of inner membrane proteins

A

TIM22

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

Mediates the insertion of inner membrane proteins synthesized in the mitochondrial matrix

A

OXA complex

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

Keeps mitochondrial precursors in their unfolded confromation using ATP

A

HSP70

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

What acts as a stop-transfer sequences that prevents further translocation across IMM

A

Hydrophobic signal

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

True or false: all peroxisome proteins must be imported from the cytosol

A

True

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

House oxidative enzymes such as oxidases that produce peroxide

A

Peroxisomes

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

How are peroxisomes inolved in lipid metabolism?

A

Degrade fatty acids by beta oxidation

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

True or false: proteins imported into peroxisomes can be imported fully-folded

A

True

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

Proteins involved in the generation or maintenace of peroxisomes

A

Peroxins

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

helps insert and fold beta-barrels in the OMM

A

SAM

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

Protein that binds to emergent signal sequences, halts translation, and targets the complex to the ER

A

Signal recognition particle (SRP)

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

How are SRPs recognized on the ER membrane?

A

SRP receptor

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

Protein translocation channel of the ER

A

Sec61 complex

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

ER chaperone that binds and releases proteins to maintain directionality

A

BiP

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

Protease that removes signal sequences in the ER membrane

A

Signal peptidase

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

-COOH-terminus in the cytoplasm

A

Type I membrane protein

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

-NH3-terminus in the cytoplasm

A

Type II membrane protein

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

What protein charges typically remain in the cytosol?

A

Positive

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

An ER lumenal Hsp70 homolog that binds to unfolded proteins and prevents aggregation

A

BiP

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

Calcium-binding proteins that are lectins that bind to oligosaccharides on incompletely folded proteins and prevents aggregation

A

Calnexin, calreticulin

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

Enzyme that aids in folding by helping correct disulfide bond formation in newly synthesized proteins

A

Protein disulfide isomerase (PDI)

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

Covalent addition of sugars to proteins

A

Glycosylation

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

Attachment of sugar to the hydroxyl group of serine on threonine

A

O-linked glycosylation

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

Attachment of sugar ot the amide nitrogen of asparagine

A

N-linked glycoslyation

44
Q

Enzyme that transfers an oligosaccharide to the Asn residue

A

Oligosaccharyl transferase (OST)

45
Q

Lipid scaffold that helps transfer sugars to proteins

A

Dolichol

46
Q

Why are sugars added to proteins in the ER

A

As a tag to mark the state of protein folding

47
Q

ER resident enymze that removes glucose in order to allow a protein to continue folding

A

Glucosidase

48
Q

Adds a single terminal glucose to a protein that is not properly folded

A

Glucosyl transferase

49
Q

Cytoslic degradation machinery

A

Proteasome

50
Q

ER resident protein sequence

A

HDEL or KDEL

51
Q

Protein coat used for Golgi -> PM and endocytosis

A

Clathrin

52
Q

Protein coast used for intragolgi and retrograde Golgi -> ER

A

COPI

53
Q

Protein coat for ER -> Golgi

A

COPII

54
Q

Coat subunit that has enzymatic activity for COPI

A

ARF

55
Q

Coat subunit that has enzymatic acitivty for COPII

A

SAR1

56
Q

Stimulate GTPase activity and make it go faster

A

GAP (GTPase activating protein)

57
Q

Molecule that initiates the formation of vescile budding on the ER membrane

A

SAR1

58
Q

When SAR1 is off, where is its helix?

A

Tucked away

59
Q

When SAR1 is on, where is its helix?

A

Exposed and inserted into phopholipid bilayer

60
Q

How does SAR1 initiate budding?

A

Nucleates the binding of coat proteins

61
Q

Two dimeric subunits of COPII coat

A

Sec23/Sec24

62
Q

Interacts with integral membrane proteins that aids in the selection of membrane integral cargo receptors

A

Sec24

63
Q

Forms a cage structure to deform the membrane and form a vesicle

A

Sec13/Sec31

64
Q

What happens when SAR1 cleaves its GTP to GDP?

A

Leaves coated vesicle, starting a cascade that uncoats the vesicle

65
Q

2 addressing systems for vesicles

A

Tethering, docking

66
Q

How many proteins are in the complex involved in the tethering process?

A

5-10

67
Q

Protein that mediates the communication between a vesicle and a membrane

A

Rab proteins

68
Q

What kind of protein are Rab proteins?

A

G-protein

69
Q

What does a Rab protein do exactly?

A

Tells SNARE proteins that a vesicle has been “tethered” and now able to “dock”

70
Q

Responsible for the merger of two phospholipid bilayers

A

SNARE proteins

71
Q

2 proteins involved in recycling SNARE proteins

A

Adapter SNAP and chaperone NSF

72
Q

Forward traffic

A

Anterograde

73
Q

Backwards traffic

A

Retrograde

74
Q

How is the localization of the golgi in perinuclear region maintained?

A

Microtubules

75
Q

Some proteins getting packaged into ER vesicles just because they are in the right place at the right time

A

Bulk Flow

76
Q

How are ER resident proteins stopped from being packaged into vesicles for transport?

A

Aggregate themselves into too large of complexes for vesicles

77
Q

Aggregation of ER proteins

A

Kin Recognition

78
Q

Fusion of uncoated vesicles in between ER and cis-Golgi

A

Vesicular tubular clusters (VTC)

79
Q

True or false: VTCs are unique to ER to golgi transport

A

True

80
Q

Fusion of vesicular membranes

A

Homotypic fusion

81
Q

Fusion of vesicular membrane to a organelle membrane

A

Heterotypic fusion

82
Q

How are KDEL sequences recognized for retrograde transport?

A

Golgi membrane bound receptor

83
Q

Motif for membrane bound residents that end up in the wrong place

A

KKXX

84
Q

What is KKXX recognized by?

A

COPI coat machinery

85
Q

How do KDEL receptors know when to unbind to its cargo?

A

Golgi is more acidic than ER, so releases in the more neutral environment of the ER

86
Q

4 functions of golgi

A

Glycosylation, production of proteoglycans, protein sorting, sulfation

87
Q

Specifically, what kind of glycosylation occurs in the golgi?

A

Modification of existing N-linked sugar, O-linked glycoslyation

88
Q

4 functions of protein glycosylation

A

Aid in protein folding, surface coating, specific interactions, ECM

89
Q

How does surface coating of glycosylated proteins help the protein

A

Protection from extracellular enivornment

90
Q

2 classes of N-linked sugars

A

High mannose, complex

91
Q

Where are high mannose sugars added?

A

ER

92
Q

Where are complex sugars trimmed?

A

Golgi

93
Q

What modifies complex sugars?

A

Glycosyltransferases

94
Q

Example of a sugar with a negative charge

A

Sialic acid

95
Q

What residues does o-linked sugar modification take place on?

A

Serine or threonine hydryoxyl residues

96
Q

Primary degradative organelle of the cell

A

Lysosomes

97
Q

Besides degradation, what other role does lysosomes play

A

Osmolyte storage

98
Q

Role of vacuoles in a plant

A

OSmotic stability or turgor pressure

99
Q

Sorting signal of proteins of secretory pathway to lysosomes

A

Mannose-6-phosphate sorting signal

100
Q

What kind of singal is the Mannose-6-phosphate signal?

A

Signal patch

101
Q

What is the mannose-6-phosphate sorting signal recognized by?

A

N-acetylglucosamine (GlcNAc) phosphotransferase in the cis-Golgi

102
Q

How does GlcNAc-P work?

A

Binds high mannose and a UDP-GlcNAc and catalyzes transfer of GlcNAc phosphate to terminal mannose residue

103
Q

How are GlcNAc sugars removed?

A

Glycosidase

104
Q

What is the mannose 6-P tag recognized by?

A

Mannose 6-phosphate receptor (M6PR) in TGN

105
Q

How are lysosome proteins released into the lysosome?

A

pH sensitivity (lysosome very acidic)

Cell Biology (7 decks)

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