Difference between revisions of "Signaling Pathway And Proteins"
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=== Adaptors === | === Adaptors === | ||
==== [http://en.wikipedia.org/wiki/GRB2 GRB2] ==== | ==== [http://en.wikipedia.org/wiki/GRB2 GRB2] ==== | ||
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| + | ==== [http://en.wikipedia.org/wiki/BCAR1 '''p130Cas/BCAR1'''] ==== | ||
| + | p130Cas/BCAR1 is an adaptor protein that regulates multiple signaling pathways leading to cell adhesion, migration, invasion, apoptosis, hypoxia and mechanical forces. p130Cas/BCAR1 plays a role in cell transformation and cancer progression and alterations of p130Cas/BCAR1 expression and the resulting activation of selective signalling are determinants for the occurrence of different types of human tumors. | ||
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| + | ==== [http://en.wikipedia.org/wiki/Paxillin Paxilin] ==== | ||
| + | The N-terminal region of paxillin is rich in protein–protein interaction sites. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, structural proteins and regulators of actin organization. The C-terminal region consists of four tandem LIM domains. | ||
Latest revision as of 17:43, 13 March 2015
Contents
Adaptors
GRB2
p130Cas/BCAR1
p130Cas/BCAR1 is an adaptor protein that regulates multiple signaling pathways leading to cell adhesion, migration, invasion, apoptosis, hypoxia and mechanical forces. p130Cas/BCAR1 plays a role in cell transformation and cancer progression and alterations of p130Cas/BCAR1 expression and the resulting activation of selective signalling are determinants for the occurrence of different types of human tumors.
Paxilin
The N-terminal region of paxillin is rich in protein–protein interaction sites. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, structural proteins and regulators of actin organization. The C-terminal region consists of four tandem LIM domains.
