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Biochem block 3 > signal transduction 3 > Flashcards

signal transduction 3 Flashcards

1
Q

Hydrophobic hormones

A

ligand for intracellular receptor

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2
Q

NT

A

ligand for Ligand-Gated Ion Channel and G pro coupled receptor

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3
Q

GF

A

ligand for EnzymeLinked and cytokine receptor

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4
Q

hormones and GF

A

ligand for EnzymeLinked receptor

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5
Q

Cytokines Growth factors

A

ligand for cytokine receptor

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6
Q

Hormones Cytokines

A

ligand for G-ProteinCoupled

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7
Q

only receptor on cytoplasm/ nucleus

A

intracell receptor (all others are on cel surface)

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8
Q

Dimeric/tetrameric complex of transmembrane polypeptides with intracellular catalytic domain

A

intracell receptor

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9
Q

 Activates autophosphorylation

A

intracell receptor

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10
Q

 Single polypeptide with 7 trans- membrane domains 

A

G-ProteinCoupled

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11
Q

Activates trimeric G protein

A

G-ProteinCoupled

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12
Q

Multimeric ring-like complex of 3-5 polypeptides with multiple transmembrane domains

A

Ligand-Gated Ion Channel

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13
Q

tf Ligand-GatedIon Channel lack transmembrane domain

A

F has it

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14
Q

Opens internal water-filled pore

A

Ligand-GatedIon Channel

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15
Q

Polypeptide dimer with DNA- binding domains

A

intracell receptor

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16
Q

Binds as dimer to DNA sequence

A

intracell receptor

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17
Q

Activates cytoplasmic enzymes

A

cytokine receptor

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18
Q

Multimeric complex of trans- membrane polypeptides lacking intrinsic catalytic activity

A

cytokine receptor

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19
Q

Tf cytokine receptor has intrinsic cat. activity

A

F lacks it

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20
Q

SH2 domain

A

2 α-helices flanking β-sheet (antiparallel)

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21
Q

β-barrel (antiparallel) followed by C-term α-helix  Binds in cleft between helix and strands

A

PTB domian

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22
Q

Binds in deep pocket lined with + residues

A

SH2

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23
Q

Binds in cleft between helix and strands

A

PTB domain

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24
Q

SH3 domain

A

Binds in shallow hydrophobic pocket

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25
Q

β-barrel fold (2 antiparallel β-sheets)

A

SH3 domain

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26
Q

2 perpendicular β-sheets (antiparallel) followed by C-term amphipathic α-helix

A

PH domain

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27
Q

PH domain

A

Binds in cleft between loops connecting strands

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28
Q

binding affinity phos. tyrosines

A

sh2 and ptb

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29
Q

bidning affinity of prolines

A

SH3 domain

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30
Q

phos. inositol PL binding affinity

A

PH domain

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31
Q

Receptors have an appropriate—- —– (dissociation constant, KD ) for the signaling molecule in order to detect it at the likely ——- in the vicinity of the cell.

A

Receptors have an appropriate binding affinity (dissociation constant, KD ) for the signaling molecule in order to detect it at the likely concentration in the vicinity of the cell.

criteria 1 of receptors

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32
Q

Receptors transmit the —- of the signaling molecule by modulation of further—– in the signaling cascade.

A

Receptors transmit the message of the signaling molecule by modulation of further components in the signaling cascade.

Criteria 2 of receptor

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33
Q

Receptors display ——- by detecting only those signaling molecules which the cell wants to perceive.

criteria 3 of reeptors

A

Receptors display specificity by detecting only those signaling molecules which the cell wants to perceive

criteria 3 of receptor

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34
Q

Nicotinic Acetylcholine Receptor

A

cationic selective

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35
Q

subunits of nicotinic ach receptor

A

Subunit with 4 transmembrane domains – M1, M2 (amphipathic), M3, and M4 – and 2 intracellular loops

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36
Q

tf both the N and C terminal in the nicotinic ach receptor is in the extracell space

A

T

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37
Q

termination of ligand gated ion channel

A

Diffusion away from the receptor and synaptic gap Degradation by enzymes on the cell surface (e.g., acetylcholinesterase)

 Re-uptake into the pre-synaptic neuron

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38
Q

Formation of an —— ligand—— state (non—– form of receptor inactivation) ensures very —- periods of signal transduction.

A

Formation of an inactive ligand-bound state (noncovalent form of receptor inactivation) ensures very brief periods of signal transduction.

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39
Q

ligand gate ion channel term.

A
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40
Q

Small ligands bind in pocket.

Large ligands bind to extracellular loops.

A

GPCR

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41
Q

GPCR has – transmembrane alpha helixes

A

7

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42
Q

tf the N terminal is on ext side and C terminal in on the int. side in GPCR.

A

T

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43
Q

glycosylation ; phosphorylation in GPCR

A

N; C terminal in GPRC

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44
Q

rhodopsin recptor

A

GPCR

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45
Q

Largest subunit in gpcr

A

alpha

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46
Q

phillic to phobic on gpcr

A

alpha; betay on gpcr

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47
Q

Guanine nucleotide-binding site (GDP, GTP) and GTPase activity

A

alpha subunit of GPCR

48
Q

GPCR portion that interacs with effector protein

A

alpha subunit

49
Q

BY unit of GPCR

A

cov attach to membrane with some int. with effector protein

50
Q

after ligand bidns GPCR —- —–,

GDP/GTP exchange causes—– with —– to dissociate

A

conf change

alpha subunit with GTP

(GPCR)

51
Q

seconary enzyme in GPCR

A

will bing alpha subunit with GTP

and intrinsic GTPase activation cause Hydrolysis of GTP to GDP and release of alpha GDP

52
Q

major mechanism of desensitization of GPCR

A

Receptor phosphorylation by protein kinases

53
Q

Protein kinase A (PKA) receptor

protein kinases (GRKs) receptor

A

+/- ligand GPCR-specific

+ ligand

54
Q

Extracellular enzymes —– or —- many of the small ligands.

A

Extracellular enzymes metabolize or inactivate many of the small ligands.

GPCR inact

55
Q

—— —— endocytosis accounts for some desensitization

A

Receptor-mediated endocytosis accounts for some desensitization

GPCR inact.

56
Q
A

Extracellular enzymes metabolize or inactivate many of the small ligands.

57
Q
A

Receptor phosphorylation by protein kinases

GPCR termination

58
Q

Caffeinated Alcohol Drinks

—– Binds to allosteric binding site on GABA-bound receptor

A

ethanol

59
Q

TF in : Caffeinated Alcohol Drinks

EToh bidning to GABA receptor keeps it closed

A

F keeps it open

60
Q

Effect of EToh on GABA bidning site

A

Causes membrane potential to become more negative

Increases GABA’s suppression of neural activity

Increases dopamine release

61
Q

GABA Ligand-Gated Ion Channel

A

Anion-Selective (Inhibitory)

62
Q

Adenosine G-Protein-Coupled Receptor thru caffiene stimulant

A

① Blocks adenosine binding site (antagonist)

63
Q

Normally Adenosine G-Protein-Coupled Receptor

A

Suppresses neural activity; increases blood flow

64
Q

Allows increased neural activity Leads to blood vessel constriction, epinephrine release, and increased level of alertness

A

Caffiene blocking

65
Q

Individual feels sober when highly intoxicated.

A

end result of cafffiene alcohol drinks

66
Q

Each subunit is a single polypeptide chain consisting of: Large extracellular N-terminal domain for binding ligand Single transmembrane domain

Intracellular C-terminal domain with catalytic domains

A

Enzyme-Linked Receptor

67
Q

dimer; tetramer

A

RTK; SER threonine kinase

68
Q

RTK

A

Ligand binding Dimerization Kinase activation

then

Autophosphorylation of tyrosine residues (cross-phosphorylation)

69
Q

GF binding to RTK

A

act of RTK bidning of adaptor pro.

then

RAS act protein

70
Q

RAS GDP

A

attaches to membrane

and is converted to active RAS (GTP) upon act of RTK by GF

RAS act protein phos it.

71
Q

(serine/threonine kinase

A

MAP Kinase Kinase Kinase

MAP Kinase – Effector Protein

72
Q

MAP Kinase Kinase Kinase

A

act by RASGTP

73
Q

threonine/tyrosine kinase)

A

MAP Kinase Kinase

74
Q

effect of MAP Kinase – Effector Protein

A
75
Q

Receptor Serine/Threonine Kinase

Ligand binding to type –

Dimerization with type –

Kinase activation

and cross-phosphorylation (Ser/Thr residues) of type —

A

Ligand binding to type II

Dimerization with type I

Kinase activation

and cross-phosphorylation (Ser/Thr residues) of type I

76
Q

upon act of receptor Serine/Threonine Kinase

A

SMAD binding and

phosphorylation

SMAD unfolding

and act

77
Q

after act of SMAD

A

dissociation and dimerization with diff SMAD subtypes

translocate to nucleus to alter gene expression

78
Q

binding of act SMAD to another SMAD

A

Exposure of nuclear localization signal (NLS)

79
Q

Termination of Enzyme linked receptor

A

Receptor-Mediated Endocytosis (Down-Regulation)

80
Q

clustering

adaptin binding

clathrin binding

A

adaptin binding

clathrin binding

clustering

81
Q

clathrin polymerization accompanied by

A

vacuole formation in Enzyme-Linked Receptor term.

82
Q

Release of — —-vesicle into cytoplasm

 Shedding of ——- ———

 Fusion of vesicle with ——– (internal —– ph)

A

Release of clathrin-coated vesicle into cytoplasm

Shedding of clathrin coat  Fusion of vesicle with endosome (internal acidic ph

3rd step in Enzyme-Linked Receptor

83
Q

tf in Enzyme-Linked Receptor: Termination

Potential recycling of receptors to plasma membrane is not possible

A

F

recycling happens at end

and

Transfer of remaining contents to lysosomes for degradation

84
Q

tf Cytokine cant recruit manyintracellular signaling proteins

A

F it can recruit a broad range because of itts great diversity

85
Q

tf the intracellular enzymatic activity has no intrincic enzymatic activity

A

t

86
Q

single polypeptide

A

cytokine receptor

87
Q

Cytokine receptor

A

multimeric complexes

88
Q

1st step of Cytokine Receptor action

A

Cytokine binding Dimerization

JAK activation and cross-phosphorylation Subunit phosphorylation

89
Q

STAT binding

A

prompts Phos Jak to phosphorylate it

90
Q

2 thing phos in cytokine receptor activation

A

JAKS and subunits

91
Q

upon sTAT phosphorylation

A

STAT dimerize

AND

Translocation to nucleus Altered gene expression

92
Q

Protein phosphatases remove —- phosphates from the receptor and/or activated —–

A

Protein phosphatases remove tyrosine phosphates from the receptor and/or activated STATs.

Cytokine receptor termination

93
Q

SOCS (suppressor of cytokine signaling)

A

inhibit STAT phosphorylation by binding

inhibiting JAKs or competing with STATs for phosphotyrosine binding sites

94
Q

Multimeric formation of the receptor after ligand binding triggers —– of the ligand-receptor complex.

A

Multimeric formation of the receptor after ligand binding triggers endocytosis of the ligand-receptor complex.

cytokine receptor termination

95
Q

importin α5

A

subunit of importin α5-β complex

96
Q

Ran-GTP

A

dissociates

STAT1 dimer (NLS) and importin α5 complex

(happens in nucleus)

97
Q

after dissociation of STAT 1 and importin a5

the STAT1 dimer

A

binds to DNA targets

and causes Expression of antiviral response

98
Q

VP24 protein from EBola

A

Competes with STAT1 dimer for binding site on importin α5 subunit

99
Q

VB24 and importin α5 subunit complex

A

diffuse thru nuclear pore

and Dissociated by complex by Ran-GTP

100
Q

Suppression of antiviral response

A

promoted by VP24 protein after Dissociation from complex by Ran-GTP

101
Q

Small KD

A

Receptor has high affinity for ligand.

102
Q

Kd=

A

koff/ kon

103
Q

LR=

A

([R]o [L]o) /(KD + [L]o)

104
Q

Bound

A

B max(Free/Free+Kd)

105
Q

Free = KD,

A

then Bound = 0.5 Bmax

106
Q

if free>Kd

A

bound= bmax

107
Q

Negligible ligand depletion (bound < 10% of free)  Negligible inactivation of ligand and receptor

A

2 conditions of saturation binding relation

108
Q

tf 2 conditions of saturation bidning relation all ligand and receptor act and there are few cell surface interaction

A

F

Negligible inactivation of ligand and receptor

Negligible cell surface interactions

109
Q

main condition of saturation plot

A

Equilibrium conditions

110
Q

Homogeneous,——-(1:1) populations of ligand and receptor

A

Homogeneous, monovalent (1:1) populations of ligand and receptor

Saturation Plot

111
Q

Label the saturation plot

A
112
Q

If EC50 >KD

Cell expresses more receptors than required for effective biological responses.

A

F

expresses less

EC50 is Half-Maximal Effective Conc

113
Q

advantage of scatchard plot

— evaluation is easy for checking original — (straight line) or comparing different — or receptors.

A

Visual evaluation is easy for checking original assumptions (straight line) or comparing different ligands or receptors.

114
Q

—- on both axes magnifies experimental error.

A

“Bound” on both axes magnifies experimental error.

disadvantage of scatchard plot

115
Q

what does this indicate abt parotid

A

KD are same but control has more Bmax than parotid

meaning;

binding characteristics of salivary gland muscarinic acetylcholine receptors of the parotid contribute to reduced saliva stimulation

116
Q

what does this indicate abt SM gland

A

Diabetic has greater KD

but = B max

no conconclusion on whether

binding characteristics of salivary gland muscarinic acetylcholine receptors of SM gland contribute to reduced saliva stimulation or not?

Biochem block 3 (12 decks)

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