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Cell Biology > Final 3 > Flashcards

Final 3 Flashcards

1
Q

Exocytosis that requires an external signal, a specific sorting signal on the vesicles, a clathrin coat, and increase of calcium

A

Regulated exocytosis

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2
Q

Exocytosis that serves to release components of ECM or just deliver newly PM proteins

A

Constitutive exocytosis

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3
Q

Why would a lysosome deposit its contents outside the cell?

A

Defense mechanism

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4
Q

Mark organelles and membrane domains in late secretory pathway

A

Phsophoinositides

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5
Q

What adds a phosphate onto the inositol ring of phosphatidylinositol

A

Lipid kinase

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6
Q

What removes a phosphate on the inositol ring of phsophatidylinositol?

A

Lipid phosphatase

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7
Q

How is neurotransmitter secretion very rapid?

A

Regulated by calcium

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8
Q

WHere does proteolytic processing occur?

A

Late Golgi

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9
Q

What holds SNARE proteins “partially-zipped up”

A

Complexin

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10
Q

Calcium snesor protein that allows the release of vesicle content by membrane fusion

A

Syanptotagmin

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11
Q

Example of compound exocytosis which provides a very large release of material over a short period of time

A

Histamines from mast cells

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12
Q

What kind of cells contain GLUT4

A

Insulin responsive cells (adipose, muscle)

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13
Q

Two compositionally distinct and different PMs

A

apical, basolateral

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14
Q

Where is the decision of what membrane a vesicle should go to in a polarized cell made?

A

TGN or all go to one membrane, and undergo endocytosis and sorting

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15
Q

How is iron transported into the cell?

A

Transferrin receptor

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16
Q

Fluid-phase endocytosis for uptake of fluids and solutes

A

Pinocytosis

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17
Q

Coat protein responsible for majority of vesicular traffic between TGN and PM

A

Clathrin

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18
Q

Composition of clathrin coats

A

Triskelion: 3 heavy chains and 3 light chains

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19
Q

Coat used for pinocytosis

A

Caveolae

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20
Q

Polyhedral superstructures that clathrin triskelion form

A

Cages

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21
Q

GTPase that constricts the neck of a newly formed coated pit to form a vesicle

A

Dyanmin

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22
Q

How is a clathrin coat removed?

A

HSP70 family of chaperones and its ATPase actiity

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23
Q

Storage form of cholesterol and primary vehicle for cholesterol transport in blood

A

Low-density lipoprotein (LDL)

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24
Q

Where in the cell are LDL particles broken down?

A

Lysosome

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25
Q

Clusters of LDL receptors in the PM

A

Coated pits

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26
Q

What does the cytosolic portion of LDL receptors do once associated with clathrin adapters?

A

Nucleates binding of a few clathrin triskelions to form coated pit

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27
Q

What happens to LDL receptors after endocytosis

A

Recycled into PM

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28
Q

How is LDL freed from its receptor?

A

pH change due to endosome

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29
Q

Separates and sequesters material to be degraded from material to be recycled

A

Mulitvesicular bodies (MVBs)

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30
Q

How are proteins recognized as needed to be degraded in MVBs?

A

Monoubiquination

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31
Q

Cytosolic protein complex that results in a specific accumulation of tagged protein into endosomal membrane invagination

A

ESCRT proteins

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32
Q

Ingestion of large particles restricted to macrophages and neutrophils

A

Phagocytosis

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33
Q

Movement of endocytosed material across the entire clel in membrane enclosed compartment

A

Transcytosis

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34
Q

What do cells unstimulated by insulin do?

A

Import glucose through the transporter

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35
Q

What do cells stimulated by insulin do?

A

Release glucose through exocytosis

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36
Q

Chemical bond formation linked to membrane transport process

A

Chemiosmotic coupling

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37
Q

High-energy electrons from NADH used to set up a proton gradient across IMM

A

Electron transport chain

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38
Q

Beta-barrel proteins on OMM

A

Porin

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39
Q

What size molecules are porins permeable to?

A

<5,000 daltons

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40
Q

Location of TCA and the source of NADH

A

Matrix

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41
Q

What is the movement of mitochondria mediated by?

A

Microtbulues

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42
Q

What generates more energy, FADH2 or NADH?

A

NADH

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43
Q

How many electrons does a NAD+ accept?

A

2

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44
Q

iElectrochemical gradient of protons in the mitochondria

A

Proton motive force (PMF)

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45
Q

What is the real name for ATP synthesis via electron transport chain

A

Oxidative phosphorylation

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46
Q

What does the complete oxidation of one glucose yield?

A

2 NADH, 2 ATP, 2 pyruvate

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47
Q

What are 2 pyruvates oxidized to?

A

8 NADH, 2 FADH, 2 GTP

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48
Q

How many ATPs are produced per glucose?

49
Q

What kind of pump is ATP synthase?

A

F-type ATPase

50
Q

Mobile electron carrier that can carry 1 or 2 electrons and is embedded into the membrane

A

Uniquinone

51
Q

How is uniquinone embedded into the membrane?

A

Isoprenoid

52
Q

What does uniquinone shuttle electrons to and from

A

From complex I to complex III

53
Q

Soluble protein with bound heme group

A

Cytochrome c

54
Q

What does cytochrome c shuttle electrons to and from

A

complex III to complex IV

55
Q

Name of complex I

A

NADH dehydrogenase

56
Q

Name of complex III

A

Cytochrome bc1

57
Q

Name of complex IV

A

Cytochrome oxidase

58
Q

Uncouple electron transport from ATP synthesis

A

Proton ionophores

59
Q

2 examples of uncouplers

60
Q

Part of ATP synthesase that is intermembrane

61
Q

Part of ATP synthesase that surrounds stalk with 6 subunits

62
Q

Name of complex II

A

Succinate dehydrogenase

63
Q

What does complex II do?

A

Accepts two electrons from succinate

64
Q

Signaling to self

65
Q

Local signaling to a close group of cells

66
Q

Signaling distributed throughout bloodstream

67
Q

Signaling based on physical contact

A

Contact dependent signaling

68
Q

Difference between endocrine and synaptic signaling

A

Endocrine are long-livd

69
Q

Most direct path of ligand signaling

A

Intracellular receptors (e.g. steroid hromones)

70
Q

Why are steroid hormones able to use intracellular receptors?

A

They are lipid soluble so can pass right through PM

71
Q

4 examples of small G-proteins

A

Ras, Rab, Rho, Ran

72
Q

How many transmembrane domains do G-protein receptors have?

73
Q

What happens when GDP-bound g-proteins are turned on?

A

ALpha dissociates from beta-gamma

74
Q

What is the alpha subunit of g-proteins postranslationally modified by?

A

Myristic acid

75
Q

What is the gamma subunit of g-proteins postranslationally modified by?

A

Polyisoprenoid

76
Q

Enzymes that have their activity modulated by interaction with a g-protein

A

G-protein effectors

77
Q

Enzyme that converts ATP to cAMP

A

Adenylyl cylcase

78
Q

cAMP initiates a protein kinase cascade by activating what?

A

Protein Kinase A (PKA)

79
Q

3 functions of cAMP

A

cortisol secretion from adrenal cortex, glycogen breakdown in muscle and liver, triacylglycerol breakdown in fat

80
Q

In muscles, what does PKA activation lead to?

A

Activation of phosphorylase kinase, leading to glycogen breakdown

81
Q

What gene regulatory protein does PKA activate?

A

cAMP regulatory element binding protein (CREB)

82
Q

What does CREB do?

A

Changes transcription of genes that contain a cAMP regulatory element (CRE)

83
Q

Enzyme that cleaves (PI(4,5)P2) into diacylglycerol and IP3

A

Phospholipase C-beta

84
Q

What does formation of IP3 do?

A

Opens Ca channel and releases Ca into the cytosol from ER

85
Q

After opening by IP3, what does released Ca bind to?

A

Protein Kinase C (PKC)

86
Q

Where are Ca concentrations kept high?

A

ER and outside cell

87
Q

Regulatory Ca binding protein for muscle contraction

A

Troponin C

88
Q

Calcium sensor for neutrotransmission

A

Synaptotagmin

89
Q

Multipurpose calcium receptor involved in many responses

A

Calmodulin

90
Q

Structure of calmodulin

A

Four EF hands (ca binding domains)

91
Q

Main targets of calmodulin

A

Protein kinases

92
Q

Protein kinase involved in smooth muscle contraction

A

Myosin light chain kinase

93
Q

Protein kinase inolved in glycogen breakdown

A

Phosphorylase kinase

94
Q

Calcium-dependent protein kinase whose activity persists even after the calcium signal has faded

A

CaM Kinase II

95
Q

How does ca-calmodulin activate CaM Kinase II?

A

BInds to inhibitory domain, liberating it

96
Q

Single-span membrane proteins that oligomerize in response to ligand binding

A

Receptor tyrosine kinases (RTKs)

97
Q

What kind of protein is the insulin receptor?

A

Disulfide-linked heterotetramer

98
Q

What kind of protein are RTKs?

99
Q

What is the typical method of oligomerization that RTKs undergo?

A

Dimerization

100
Q

What does receptor oligomerization of RTKs lead to?

A

Activation of kinase domain by autophosphorylation

101
Q

What happens once RTKs become autophosphorylated?

A

Receptor increases its kinase activity towards substrates

102
Q

Binds specifically to phosphotyrosine in RTKs

A

Src Homology Region 2 domain (SH2)

103
Q

Binds to proline rich motifs in RTKs

A

Pleckstrin Domain (PH)

104
Q

What membrane lipid do PH domains associate with?

105
Q

3 enzymes recruited to PDGF receptor by its SH2 domain

A

PI3 kinase, Ras GAP, PLC-gamma

106
Q

Primary target of Ras

107
Q

What cascade is Raf-1 the first element of?

A

MAP kinase

108
Q

Signal that tells a cell to divide

109
Q

Through what molecule does Ras activation generate new membrane lipids?

A

PI 3-kinase

110
Q

Receptors that rely on its associated kinases to cross phosphorylate one another

A

Tyrosine kinase associated receptors

111
Q

Target of Jak kinases

112
Q

Role of STAT

A

Regulator of gene expression

113
Q

What kind of receptors do TGF-beta use?

A

Serine/threonine kinases

114
Q

Activated TGF-beta activates what kind of gene regulatory proteins?

115
Q

Ligands for receptor guanylyl cyclases

116
Q

What do ANP and BNP do?

A

Regulate salt and water balance

117
Q

What does cGMP activate?

118
Q

Membrane bound singaling protein expressed on developing nerve cells

119
Q

Receptor of Delta

Cell Biology (7 decks)

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