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PMID: 7519780 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Src kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 16 ·1994-08-02 ·Pages 7477-81

Møller NP, Møller KB, Lammers R, Kharitonenkov A, Sures I, Ullrich A

Abstract

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 pp60src.

MeSH Terms
Amino Acid Sequence Cytoskeletal Proteins Humans Molecular Sequence Data Muscles Phosphoproteins/genetics Protein Tyrosine Phosphatase, Non-Receptor Type 3 Protein Tyrosine Phosphatases/genetics,metabolism Protein-Tyrosine Kinases/metabolism Proto-Oncogene Proteins pp60(c-src)/metabolism RNA, Messenger/analysis Sequence Homology, Amino Acid Tissue Distribution
Chemicals
Cytoskeletal Proteins Phosphoproteins RNA, Messenger ezrin Protein-Tyrosine Kinases Proto-Oncogene Proteins pp60(c-src) PTPN3 protein, human Protein Tyrosine Phosphatase, Non-Receptor Type 3 Protein Tyrosine Phosphatases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Møller N P
Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Germany.
Møller K B
Lammers R
Kharitonenkov A
Sures I
Ullrich A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.16.7477
Published
1994-08-02
Pages
7477-81
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC44424
Subset
IM
Databases
GENBANK
X79510
External Links
PubMed source DOI: 10.1073/pnas.91.16.7477 PMC Full Text View journal details
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