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bio 340 > Cell Signalling > Flashcards

Cell Signalling Flashcards

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Biology 101 flashcards
1
Q

what are some types of effector proteins?

A

transcription factor, cytoskeleton proteins, metabolic enzymes

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2
Q

signals can tell the cell to

A

survive, grow+divide (mitosis), differentiate, D I E

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3
Q

plasma membrane is impermeable to ______ molecules

A

hydrophobic

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4
Q

what are the two types of delivery signals?

A

cell-surface receptors and intracellular receptors

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5
Q

what are intracellular receptors?

A

carrier proteins brings a small hydrophobic to the cell and goes through the membrane

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6
Q

what are cell-surface receptors?

A

signal molecule arrives at a receptor protein that will relay signal to the inside

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7
Q

what are the 5 forms of intracellular signaling based on distance?

A

contact-dependent, paracrine, synaptic, autocrine, endocrine

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8
Q

what is contact-dependent signaling?

A

signaling and target cell needs physical contact

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9
Q

what is paracrine signaling?

A

cell secretes signal and cells around them receive the signal with receptors

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10
Q

what is synaptic signaling?

A

cell body that can stretch and neutrotransmitter is released in synapse

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11
Q

what is autocrine signaling?

A

cell secretes a signal and binds to its own receptor

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12
Q

what is endocrine signaling?

A

cell secreting the stimulus is far so endocrine organs that secrete hormones through bloodstream

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13
Q

what are the 2 types of response once a signal is received?

A

fast- protein is ready and stimulus will alter protein (change conformation or have it interact with another protein)
slow- needs to make protein from scratch. signal will activate transcription

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14
Q

the same stimuli interacting with the different cells will

A

have a different response

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15
Q

what does acetylcholine do in the heart pacemaker cell?

A

decreased rate of firing

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16
Q

what does acetylcholine do in the salivary gland cell?

A

salivary secretion

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17
Q

what does acetylcholine do in the skeletal muscle cell?

A

contraction

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18
Q

what are the 3 major classes of transmembrane receptor?

A
  1. ion-channel linked
  2. g protein linked
  3. enzyme-linked (receptor is an enzyme itself or associated with an enzyme)
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19
Q

what is an ion-channel-coupled receptor?

A

signals change the behavior of ion channel usually opens up and lets ions inside

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20
Q

what is a g-protein coupled receptor?

A

g protein activates when signal binds to receptor (spans 7 times on membrane). g protein will act on further enzymes.

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21
Q

what is an intrinsic enzyme activity?

A

receptor itself is an enzyme

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22
Q

what is an associated enzyme activity?

A

receptor is closely associated with an enzyme

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23
Q

how does the receptor relay info to the inside?

A
  1. conformational change of receptor

2. multimerization of receptor

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24
Q

what are second messengers?

A

small diffusable molecules produced by signaling enzymes that affect target proteins

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25
Q

describe signaling by phosphorylation

A

protein kinase that does phosphorlyation

protein phosphatase reverses kinase effect

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26
Q

what is phosphorylation?

A

phosphate group taken from ATP to be put on amino acid. not necessarily activating, just changes conformation

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27
Q

what does phosphorylation?

A

altered conformation, target for protein breakdown, new protein-protein binding site

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28
Q

what is the monomeric g protein?

A

one, small g-protein

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29
Q

what is heterotriemeric g protien?

A

3 part, one part binds to g protein

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30
Q

what is subcellular localization?

A

signaling is more efficient is the necessary parties are found near each other

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31
Q

what is a scaffold protein?

A

hold enzymes that will interact with receptor

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32
Q

what is an activated receptor?

A

receptor has binding sites for necessary enzymes on cytoplasmic domain

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33
Q

what is phopsoinositide docking sites?

A

???? tiddy?

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34
Q

what are modular binding domains?

A

a protein most likely to have several modular segments

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35
Q

what are adaptor proteins?

A

proteins that are composed solely of protein-protein interaction domains. act as a link.

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36
Q

what are effector proteins?

A

protein that plays a central role in the change in cell response

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37
Q

what is positive feedback?

A

A activates B and B further activates A

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38
Q

what is negative feedback?

A

A activates B and B inhibits A

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39
Q

what is the point of receptor down-regulation/desensitization?

A

so you dont get the same response all the time

40
Q

what does epinephrine do?

A

breakdown of glycogen into glucose in the liver
breakdown of triacylglyercol to fatty acids
increase heart rate
contraction of arteries

41
Q

what subunit binds to GTP/GDP of g-protein?

A

alpha subunit

42
Q

beta and gamma work?

A

together

43
Q

describe GPCR signaling

A
  1. signaling molecule binds to GCPR ->conformational change in cytoplasmic domain.
  2. GDP dissociates and GTP arrives ->g-protein is active. beta+gamma dissociate
  3. activates effector target
44
Q

what are the 3 effector proteins?

A

adenylyl cyclase (cAMP, then PKA), rho family, PLC

45
Q

describe cAMP formation

A

ATP on alpha subunit activates adenylyl cyclase to make cAMP. ATP loses 2 phosphates and turns into AMP which is cyclic. phosphate makes bond with itself.

46
Q

what stops cAMP?

A

cAMP phosphodiesterase

47
Q

what is PKA?

A

cAMP-dependent kinase

48
Q

what happens with PKA interacts with cyclic AMP?

A

cAMP binds to regulatory subunits and lets go of catalytic subunit. the catalytic subunits are now active.

49
Q

what occurs after PKA is activated?

A

go through nucleus. phosporylates to CREB to work as a transcription regulator.

50
Q

describe mating signal process

A

mating factor binds with receptor. activates g protein. activate rho family.
rho->formin
WASp->ARP complex

51
Q

what is ARP complex?

A

nucleation of actin. binds with activating factor, and then with actin monomers to build actin cable

52
Q

what is formin?

A

found at the end of actin polymer. move as more actins bind with top to lengthen it

53
Q

PLC cuts?

A

phospholipid called PIP2 (phosphotidylide inasotiol)

54
Q

what are PIP kinases?

A

phosphorlyates PIP

55
Q

describe PLC beta signaling

A

signal molecule goes to receptor and activates g-protein than phospholipase. it cleaves PI into diacylglycerol and IP3. IP3 releases Ca ions from ER. diacylglyercol and Ca ions activate protein kinase C

56
Q

Free calcium in the cell is ____ and calcium outside is _____

A

lower, higher

57
Q

there is also a high calcium level in the ____ organelles

A

ER

58
Q

what is calmodulin?

A

calcium dependent switch. found in eukaryotic cells. binds calcium in 4 sites. undergoes conformational change when bound to calcium and target.

59
Q

what is CaM-kinase signaling?

A

calcium/calmodulin-dependent kinase. they get activated when calcium is flooded in cytosol and binds to calmodulin to activate Cam-kinase.
kinase helps phosphorylate gene regulatory proteins (turn them on)

60
Q

what is CaM-kinase II?

A

highly expressed in brain

61
Q

what is calcineurin signaling?

A

calmodulin binds to calcium activates the phosphotase, calcineurin. desphosphorylates NFAT to help it get into the nucleus to activate gene transcription

62
Q

what is EGF receptor?

A

epidermal growth factor

63
Q

what is cell growth?

A

cell growing in size

64
Q

what is cell proliferation?

A

cells dividing

65
Q

growth factors are usually _____ promoters

A

mitotic

66
Q

what is insulin receptor?

A

insulin-like growth factor

67
Q

what is NGF receptor?

A

nerve growth factor

68
Q

what is PDGF receptor?

A

platelet-derived growth factor. helps patch up wound

69
Q

what is FGF receptor?

A

fibroblast (found in connective tissue) growth factors

70
Q

what is VEGF receptor?

A

vascular endothelial (make up blood vessels) growth factor

71
Q

what does VEGF receptor have to do with cancer?

A

cancers secrete this to create pathways to the center of the tumor

72
Q

what is Eph receptor?

A

ephrin

73
Q

how do receptor tyrosine kinases work?

A

signal protein makes more than 1 receptor get close to each other. (multimerization or cross-linking)
receptors phosphorylate each other.
phosphorlyation site becomes binding sites for future molecules

74
Q

what is trans-autophosphorylation?

A

receptors of the same kind phosphorylate each other

75
Q

what is the last photoreceptor that binds to R8 in fruit flies?

A

R7

76
Q

what is sev?

A

receptor tyrosine kinase that has R7 mutation (on R7 cell)

77
Q

R7 and R8 have to ______ interact to do signaling

A

physically

78
Q

what is Boss?

A

bride of sevenless ligand for sev receptor

79
Q

describe fruit fly eye development (also applicable to RTK signaling in general)

A

boss binds to sev RTK

adaptor protein binds to receptor and brings in Ras-GEF to activate g-protein

80
Q

what is sos?

A

son of sevenless, ran-gef bound to adaptor protein thats bound with sev RTK

81
Q

what is an oncogene?

A

mutated version of a gene that makes cells proliferate like crazy

82
Q

describe the MAP kinase pathway

A

activated g protein activates MAP kinase kinase kinase.

83
Q

describe PI3K signaling

A

signal binds to receptor. phosphoinositides get phosphorylated then recruits proteins to bind to it

84
Q

what are phosphoinositides ?

A

phosphaatidylinositol that is phosphorylated at several spots

85
Q

what is PI3 kinase?

A

phosphorylates the 3rd position

86
Q

what is the cell survival signal?

A

mediated by a protein called Akt

87
Q

describe apoptosis inhibitory pathway

A

survival signal binds to receptor and then it phosphorylates PI 3-kinase to phosphorylate PIP2 into PIP3. PH domains PDK1 and Akt come in and PIP3 act as a docking site. Akt gets phosphorylated by PDK1 and mTOR and dissociates from the membrane and it takes away the inactive inhibitory apoptosis protein from Bad. the apoptosis inhibitor is now active and inhibits apoptosis properly. the Bad protein binds with the 14-3-3 and is now inactive

88
Q

what is rapamycin?

A

transplantation rejection drugs, used as an immunosuppressant. inhibits cell proliferation

89
Q

rapamycin interacts with

A

TOR (target of rapamycin) and stops it

90
Q

what is TOR?

A

activates ribosomes to do translation, cause ribosome synthesis.

91
Q

what is Tsc2?

A

inhibits Rheb

92
Q

what is Rheb?

A

activates mTOR

93
Q

describe mTOR regulation without growth factor

A

active Tsc2->inactive Rheb->inactive mTOR-> no cell growth

94
Q

describe mTOR regulation with growth factor

A

active PI3 kinase->active Akt -> inhibits Tsc2->active Rheb -> active mTOR-> cell growth

95
Q

what is JAK?

A

jack family of kinases

96
Q

what are cytokines?

A

hormones that immune system uses to talk to each other

97
Q

describe JAK/STAT pathway

A

cytokine receptors are already attached to JAK. when cytokine binds to receptors they will multimerize and JAK will trans-phosphorylate to become active. they will phosphorylate the cytoplasmic domain of the receptor to become a docking site for STAT. STAT comes and binds and gets phosphorylated by JAK. phosphorylated STAT forms dimer and go to nucleus to start doing gene transcription

bio 340 (13 decks)

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