Abstract:
:Rho GTPases are molecular switches involved in the regulation of many cellular processes. This review summarizes work examining how stimulation of receptor tyrosine kinases (RTKs) leads to the activation of Rho guanine nucleotide exchange factors (GEFs) and their Rho GTPase substrates. The collective findings strongly suggest that RTK signaling to Rho proteins is a general signal transduction mechanism, like RTK mediated activation of phosphatidyl inositol 3-kinase, phospholipase Cgamma, and the mitogen activated protein kinase (MAPK) pathway. More than half of the 58 known human RTKs activate at least one Rho family member. Likewise, 16 Rho GEFs directly interact with and/or are phosphorylated by a RTK. The specificity of receptor tyrosine kinase/Rho GEF signaling seems to be somewhat promiscuous. There several cases where multiple RTKs activate the same Rho GEF and where a single RTK can activate multiple Rho GEFs. Expression analysis indicates that the average human tissue contains transcripts for 33 RTKs, 34 Rho GEFs, and 14 Rho GTPases with each tissue containing a unique complement of these proteins. Given the promiscuity of RTKs for Rho GEFs, Rho GEFs for Rho GTPases, and the large number of these proteins expressed in cells, a complex combinatorial network of proteins in these families may contribute to coding specific signals and cell responses from RTKs.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Schiller MRdoi
10.1016/j.cellsig.2006.01.022subject
Has Abstractpub_date
2006-11-01 00:00:00pages
1834-43issue
11eissn
0898-6568issn
1873-3913pii
S0898-6568(06)00081-7journal_volume
18pub_type
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journal_title:Cellular signalling
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