SRC KINASE ASSOCIATES WITH A MEMBER OF A DISTINCT SUBFAMILY OF PROTEIN-TYROSINE PHOSPHATASES CONTAINING AN EZRIN-LIKE DOMAIN

被引:82
作者
MOLLER, NPH [1 ]
MOLLER, KB [1 ]
LAMMERS, R [1 ]
KHARITONENKOV, A [1 ]
SURES, I [1 ]
ULLRICH, A [1 ]
机构
[1] MAX PLANCK INST BIOCHEM, DEPT MOLEC BIOL, D-82152 MARTINSRIED, GERMANY
关键词
FOCAL ADHESION; CYTOSKELETON; SRC HOMOLOGY 2 AND 3 DOMAINS;
D O I
10.1073/pnas.91.16.7477
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 6.2-kb full-length clone encoding a distinct protein-tyrosine phosphatase (PTP; EC 3.1.3.48), PTPD1, was isolated from a human skeletal muscle cDNA library. The cDNA encodes a protein of 1174 amino acids with N-terminal sequence homology to the ezrin-band 4.1-merlin-radixin protein family, which also includes the two PTPs H1 and MEG1. The PTP domain is positioned in the extreme C-terminal part of PTPD1, and there is an intervening sequence of about 580 residues without any apparent homology to known proteins separating the ezrin like and the PTP domains. Thus, PTPD1 and the closely related, partially characterized, PTPD2 belong to the same family as PTPH1 and PTPMEG1, but because of distinct features constitute a different PTP subfamily. Northern blot analyses indicate that PTPD1 and PTPD2 are expressed in a variety of tissues. In transient coexpression experiments PTPD1 was found to be efficiently phosphorylated by and associated with the src kinase pp60(src).
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收藏
页码:7477 / 7481
页数:5
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