期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 25, 页码 15892-15903出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M115.640607
关键词
phosphatidylinositide 3-kinase (PI 3-kinase); phosphatidylinositol kinase (PI kinase); Raf kinase; RAS protein; small GTPase; E-RAS; effector selection; H-RAS; embryonic stem cell-expressed RAS; specificity determining residues
资金
- German Research Foundation through Collaborative Research Center 974 [SFB 974]
E-RAS is a member of the RAS family specifically expressed in embryonic stem cells, gastric tumors, and hepatic stellate cells. Unlike classical RAS isoforms (H-, N-, and K-RAS4B), E-RAS has, in addition to striking and remarkable sequence deviations, an extended 38-amino acid-long unique N-terminal region with still unknown functions. We investigated the molecular mechanism of E-RAS regulation and function with respect to its sequence and structural features. We found that N-terminal extension of E-RAS is important for E-RAS signaling activity. E-RAS protein most remarkably revealed a different mode of effector interaction as compared with H-RAS, which correlates with deviations in the effector-binding site of E-RAS. Of all these residues, tryptophan 79 (arginine 41 in H-RAS), in the interswitch region, modulates the effector selectivity of RAS proteins from H-RAS to E-RAS features.
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