Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56(lck) and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region

被引：91
作者：
Park, I
Chung, J
Walsh, CT
Yun, YD
Strominger, JL
Shin, J
机构：
[1] HARVARD UNIV,SCH MED,DEPT MOLEC PHARMACOL & BIOCHEM,BOSTON,MA 02115
[2] MOGAM RES INST,SIGNAL TRANSDUCT LAB,KYONGGI DO,SOUTH KOREA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 26期
关键词：
serine; threonine kinase; allosteric regulation;
D O I：
10.1073/pnas.92.26.12338
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
A previously undescribed 62-kDa protein (p62) that does not contain phosphotyrosine but, nevertheless, binds specifically to the isolated src homology 2 (SH2) domain of p56(lck) has been identified, The additional presence of the unique N-terminal region of p56(lck) prevents p62 binding to the SH2 domain, However, phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56(lck) SH2 domain with p62, Moreover, p62 is associated with a serine/threonine kinase activity and also binds to ras GTPase-activating protein, a negative regulator of the ras signaling pathway. Thus, phosphotyrosine-independent binding of p62 to the p56(lck) SH2 domain appears to provide an alternative pathway for p56(lck) signaling that is regulated by Ser-59 phosphorylation.
引用
收藏
页码：12338 / 12342
页数：5
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