lecture 24 redone Flashcards

1
Q

PH domain
proteins with PH domain bind to

A

phosphorylated inositol phospholipis in the plasma membrane (localises signallng)

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

PTB domain

A

binds phosphotyrosine (P-Y) residues

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

SH2 domain
2 domain binds phosphotyrosine residues surrounded by unique proetin sequences

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

SH3 binds to specfically to proline rich regions

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

insulin receptor is a tetrameric tyrosine kinase receptor

A

2alpha , 2 beta , alpha at top so binds

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

the IR is expressed as two isoforns

A

isoforn A and B

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

beta subunit has tyrosin kinase redisues meaning it can

A

phosphorylate tyrosine when activated

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

Shc - SH2 containing apapter protein
Shc has PTB and SH2 domain
shc can bind to insulin receptor, when they bind tyrosine is phosphorylates uncoveing a binding site for binding SH3 domain

A

e.g Grb2 from SH3 domain binds to Shc

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

IRS = insulin receptor substrate (adapter protein)
IRS1,2,3,4 contains a

A

PH and PTB domain

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

PH and PTB domain enable binding to phosphorylates insulin receptor, after binding the IRS becomes phosphorylated on tyrosines by

A

IR tyrosine kinase activtity

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

IRS has wq potential tyrosine phosphorylation sites

A

making it a dokcing protein for proteins with SH2 domains

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

PI3 kinase, Grb2 and SHP2

A

can bind to IRS as the have SH2 domains

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

insulin receptor is bound to by IRS which is bound to by Shc via the Grb2, interacts with

A

SOS when bound

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

SOS acts as a GDP/GTP exchange factor
ras ia inactive when bound to GDP ras is activtated when its exchanged for GTP. Ras GTP activates

A

raf

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

raf activtes

A

MAPKK

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

MAPKK activates

A

MAP- kinase whcih drives growth, differentition adn proliferation

17
Q

PI3 can bind to IRS via SH2 domain, this leads to generation of

18
Q

PIP3 is a binding parter for proteins with PH domains eg

19
Q

PI3K adds a phosphorylates PIP3

A

PDK1 binds to PIP3 and it enables the phosphorylation of a redisue on AKT

20
Q

mTORC2 phosphorylates AKT

A

dual phosphorylation activates AKT

21
Q

when AKT is phosphorylated it can phosphorylate other proteins
AS160 blocks movement of vesicles containing GLUT4 by

A

regulating Rab

22
Q

for Ran to facilitate the movement to the membrane it needs to be bound to

A

GTP when AS160 prevents them binding

23
Q

phosphorylation of AKT leads to phosphorylation of

A

AS160 leading to its inactivation causing GLUT4 to translocate

24
Q

AKT phosphorylates TSC2 which regulates

25
activation of mTORC1 activates elF4E-BP1 and S6K1 leads to translation initiation adn ribosome biogensis
protein synthesis ^
26
FOXO1 induces G6PC and PEPCK (enzymes of gluconeogenesis) and FOXO1 represses GCK (glucokinase) AKT phosphorylates FOXO1 which then translocates to the cytoplasm wheres its
ubiquitinated and degreaded allowing repression og G6PC and PEPCK and insuction og glucokinase
27
glycogen sythase kinase 3 (GSK3) is inactivates when phosphorylated by AKT, GSK when is activate is able to phosphorylate many proteins
GSK phosphorylaltes glycogen synthase making it inactive and not mych glycogen is formed AKT phosphorylates GSK3 making it inactive promoting glycogen Nand protein synthsis