Ras Isoforms Vary in Their Ability to Activate Raf-1 and Phosphoinositide 3-Kinase
摘要：
Ha-, N-, and Ki-Ras are ubiquitously expressed in mammalian cells and can all interact with the same set of effector proteins. We show here, however, that in vivo there are marked quantitative differences in the ability of Ki- and Ha-Ras to activate Raf-1 and phosphoinositide 3-kinase. Thus, Ki-Ras both recruits Raf-1 to the plasma membrane more efficiently than Ha-Ras and is a more potent activator of membrane-recruited Raf-1 than Ha-Ras. In contrast, Ha-Ras is a more potent activator of phosphoinositide 3-kinase than Ki-Ras. Interestingly, the ability of Ha-Ras to recruit Raf-1 to the plasma membrane is significantly increased when the Ha-Ras hypervariable region is shortened so that the spacing of the Ha-Ras GTPase domains from the inner surface of the plasma membrane mimicks that of Ki-Ras. Importantly, these data show for the first time that the activation of different Ras isoforms can have distinct biochemical consequences for the cell. The mutation of specific Ras isoforms in different human tumors can, therefore, also be rationalized.
展开
关键词：
Distinct Binding Domains Protein-Kinase Plasma-Membrane Phosphatidylinositol 3-Kinase Tyrosine Phosphorylation N-Ras Cells 14-3-3-Proteins Association Signal
DOI：
10.1074/jbc.273.37.24052
被引量：
年份：
1998
Elsevier
BMJ
国家科技图书文献中心
(权威机构)
Wiley
Semantic Scholar
查看更多
doi.org
掌桥科研
万方医学
dx.doi.org
Cell Press
Europe PMC
NCBI
NCBI
JBC
AACR
ResearchGate
(全网免费下载)
ResearchGate
EBSCO
jimmunol.org
jvi.asm.org
genesdev.cshlp.org
ajprenal.physiology.org
mysciencework.com
erc.endocrinology-journals.org
molbiolcell.org
jcb.rupress.org
SAGE
espace.library.uq.edu.au
molpharm.aspetjournals.org
theoncologist.alphamedpress.org
ar.iiarjournals.org
embor.embopress.org
www.socolar.com
mendeley.com
readcube.com
onAcademic
espace.library.uq.edu.au
(全网免费下载)
ResearchGate
(全网免费下载)
espace.library.uq.edu.au
(全网免费下载)
通过文献互助平台发起求助，成功后即可免费获取论文全文。
相似文献
参考文献
引证文献
来源期刊
引用走势
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用！
