chapter 14 sensory and signal transduction Flashcards

1
Q

what does epinephrine bind to

A

b-adrenergic receptor

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2
Q

which molecule is changed when a photon binds rhodopsin

A

11-cis-retinal til 11-trans retinal

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3
Q

what could be an inhibitor of epinephrin’s binding to B-adrenergic receptor

A

carazolol

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4
Q

G-protein consists of

A

3- domains
alpha binds the nucleotide (p-loop NTPase)
beta
gamma

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5
Q

What happens when GTP is bound to G protein

A

the B and Y subunits dissociate. so alpha can transmit the signal to other targets

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6
Q

one hormone-complex can stimulate the nucleotide exchange in many

A

G-proteins

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7
Q

what does cAMP activate and how does it do it

A

protein kinase A

by binding to the regulatory chains releasing the catalytic domains which are active on their own

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8
Q

what does PKA or protein kinase A consist of

A

2 regulatory chains

2 catalytic domains

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9
Q

what does PKA stimulate besides the activation of downstream targets

A

it activates the expression of specific genes by phosphorylating a transcriptional activator called the cAMP response element binding protein (CREB)

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10
Q

how is the adrenergic receptor deactivated

A

GRK2 phophorylates the carboxyl-terminal of the hormone-receptor complex
B-arrestin binds to the phosphorylated hormone receptor complex and diminishes the ability to activate G proteins

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11
Q

PIP2

A

phosphatidylinositol 4,5 bisphosphate cleaved by phosphlipase triggered by the angiotensin iI receptor, yielding diacylglycerol DAG + inositol 1,4,5-trisphosphate

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12
Q

what does DAG do

A

remains in the plasmamembrane. activates protein kinase C phosphorylating many serine and threonine residues in many protein targets. Also requires that the protein kinase C is bound to ca2+

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13
Q

what makes ca2+ able to inducee structural changes in proteins

A

because it has a capacity to be coordinated to several ligands (6-8) oxygen atoms. allowing it to cross-link different segments of a protein

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14
Q

calmodulin

A

regulatory protein four ca2+ bindingssites
EF-hands (helix loop helix)

calmodulin regulates calomodulin dependent protein kinases, that phosphorylate many targets regulating fuel metabolism, neurotransmiter synthesis, release and so on.

ca2+ coordinated by 7 oxygen atoms

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15
Q

in insulin receptor the tyrosine kinase is

A

a part of the receptor

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16
Q

the activation in insulin receptor

A

lies in the center of the structure

when the tyrosin residues are phosphorylated the activation loop crosses around making the structure more compact

17
Q

how does insulin bind and activate insulin receptors

A

approachs the space between the alpha subunits and the alpha subunits get closer to each other, which then causes the beta-subunits to approach each other and then the activation domains from each beta-subunit fits in the active site of the tyrosine kinase in the other beta-subunit causing the phosphorylation of tyrosin and giving the receptor its active conformation

18
Q

adaptor proteins are not

A

enzymes

19
Q

How is insulin signaling terminated

A

by the action of phosphatases
1- protein tyrosine phosphatase ( removing phosphoryl groups from insulin receptor and IRS)
2- Lipid phosphatase (PIP3 to PIP2)
3- protein serin phosphatase to deactivate Akt1

20
Q

what structural feature causes the dimerisation of EGF-receptors
what happens when EGF is absent

A

dimerisation arm from each subunit

the dimerisation arm is bound to its receptor preventing it from binding to the other receptor

21
Q

cross phsosphorylations in EGF-receptors

A

carboxyl-terminals rather than activation loops

22
Q

when is the kinase in egf-receptor activated

A

activated without phosphorylation

23
Q

GAPs

A

GTPase activating proteins (GAPs)

24
Q

In insulin and EGF-receptor mediated pathways

A

both act as tyrosin kinases

25
Q

pleckstrin homology domains

A

facilitate the interactions with lipid PIP3

26
Q

HER related to

A

EGFR stimulates overexpression even