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An overview of enzyme-linked membrane receptors, focusing on receptor tyrosine kinases and their role in insulin signaling. It explains how ligands bind to extracellular domains, activating intracellular catalytic domains, and initiating phosphorylation cascades. The document details the process of receptor autophosphorylation, the interaction of phosphorylated irs with protein bas, and the subsequent activation of transcription factors. It also covers the importance of glucose transporters and the implications of insulin resistance in diabetes. Useful for understanding the molecular mechanisms of cell signaling and the role of insulin in glucose metabolism. (410 characters)
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ligand-binding
Mostcommon
catalytic
domains have
tyrosine
activity*
Adds a
phosphorylation
change
allowing binding
catalytic
⑨
a
chain
s
n
acIds
phosphate group
a
M
*Some
catalytic
guanyly/cyclase activity
r
cGMP,
a
secondary
messenger
Receptor
Tyrosine
Insulin
receptor tyrosine
in
I
⑰
cells
or
to
Da
Inside
Insulin
Receptor:
Glucose
Import
Myocytes
⑪Erase an
in
an
in anin registrich
When insulin interacts
with its receptor,
vesicles more to the surface and fuse with
the
Signaling
Cascade:
Ligand Binding
plasma membrane. Increasing
the number of
glucose
transporters In the plasma membrane.
are
removed from the plasma
Insulin binds to extracellular domains
of receptor
membrane
small vesicles
activates
domain inside
cell
domain in one
residues in another receptor
allows
and
of
protein
IRS
↓
Indirect Interaction
of
IRS with
protein
Bas Initiates
a series of protein
I
kinases enters nucleus
The smaller resides
fuse with a
factor
becomes
endosome
Stimulates expression
of
Insulin levels rise again