Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains

Maayan Barnea; Tsviya Olender; Mark T Bedford; Ari Elson

doi:10.1042/BST20160141

Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains

Biochem Soc Trans. 2016 Oct 15;44(5):1295-1303. doi: 10.1042/BST20160141.

Authors

Maayan Barnea¹, Tsviya Olender¹, Mark T Bedford², Ari Elson¹

Affiliations

¹ Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.
² Department of Epigenetics and Molecular Carcinogenesis, MD Anderson Cancer Center, University of Texas, Smithville, TX 78957, USA.

PMID: 27911712
DOI: 10.1042/BST20160141

Abstract

Protein tyrosine phosphatases (PTPs) perform specific functions in vivo, despite being vastly outnumbered by their substrates. Because of this and due to the central roles PTPs play in regulating cellular function, PTP activity is regulated by a large variety of molecular mechanisms. We review evidence that indicates that the divergent C-terminal tail sequences (C-terminal domains, CTDs) of receptor-type PTPs (RPTPs) help regulate RPTP function by controlling intermolecular associations in a way that is itself subject to physiological regulation. We propose that the CTD of each RPTP defines an 'interaction code' that helps determine molecules it will interact with under various physiological conditions, thus helping to regulate and diversify PTP function.

Keywords: SH2 domain; phosphorylation/dephosphorylation; protein tyrosine phosphatases; sequence motif.

Publication types

Review

MeSH terms

Amino Acid Motifs*
Amino Acid Sequence
Animals
Binding Sites
Humans
Models, Biological
Phosphorylation
Protein Binding
Receptor-Like Protein Tyrosine Phosphatases / chemistry
Receptor-Like Protein Tyrosine Phosphatases / metabolism*
Tyrosine / chemistry
Tyrosine / metabolism*

Substances

Tyrosine
Receptor-Like Protein Tyrosine Phosphatases