Please use this identifier to cite or link to this item:
|Title:||A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42|
|Authors:||Manser, E. |
|Citation:||Manser, E.,Leung, T.,Salihuddin, H.,Tan, L.,Lim, L. (1993-05-27). A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42. Nature 363 (6427) : 364-367. ScholarBank@NUS Repository.|
|Abstract:||The Ras-related Rho subfamily of GTP-binding proteins (p21s), which includes Rho, Rac and Cdc42Hs, is implicated in different aspects of cytoskeletal organization1,2. These proteins behave like Ras (p21ras) in that their active GTP-bound form is inactivated by intrinsic hydrolysis of the nucleotide γ-phosphate, which can be stimulated by GTPase-activating proteins (GAPs). We have previously shown that there is a diversity of GAPs that recognize this subfamily3, including n-chimaerin, which is enriched in the hippocampus4; we also detected proteins that bind these p21 proteins and seem to inhibit GTP hydrolysis. We now report the characterization of a hippocampal complementary DNA encoding a tyrosine kinase that specifically binds Cdc42Hs in its GTP-bound form. This binding is mediated by a unique sequence of 47 amino acids C-terminal to an SH3 domain and inhibits both the intrinsic and GAP-stimulated GTPase activity of Cdc42Hs. Our findings indicate that there may be a regulatory mechanism that sustains the GTP-bound active form of Cdc42Hs and which is directly linked to a tyrosine phosphorylation pathway.|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Nov 16, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.