A Drosophila-centric view of protein tyrosine phosphatases

Teri Hatzihristidis; Nikita Desai; Andrew P Hutchins; Tzu-Ching Meng; Michel L Tremblay; Diego Miranda-Saavedra

doi:10.1016/j.febslet.2015.03.005

A Drosophila-centric view of protein tyrosine phosphatases

FEBS Lett. 2015 Apr 13;589(9):951-66. doi: 10.1016/j.febslet.2015.03.005. Epub 2015 Mar 13.

Authors

Teri Hatzihristidis¹, Nikita Desai², Andrew P Hutchins³, Tzu-Ching Meng⁴, Michel L Tremblay⁵, Diego Miranda-Saavedra⁶

Affiliations

¹ Goodman Cancer Research Centre, McGill University, 1160 Pine Avenue, Montreal, Québec H3A 1A3, Canada; Department of Medicine, Division of Experimental Medicine, McGill University, Montreal, Quebec, Canada.
² Goodman Cancer Research Centre, McGill University, 1160 Pine Avenue, Montreal, Québec H3A 1A3, Canada; Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
³ Key Laboratory of Regenerative Biology and Guangdong Provincial Key Laboratory of Stem Cell and Regenerative Medicine, South China Institute for Stem Cell Biology and Regenerative Medicine, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, Guangdong 510530, China.
⁴ Taiwan International Graduate Program, Academia Sinica, Taipei, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan; Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
⁵ Goodman Cancer Research Centre, McGill University, 1160 Pine Avenue, Montreal, Québec H3A 1A3, Canada; Department of Medicine, Division of Experimental Medicine, McGill University, Montreal, Quebec, Canada; Department of Biochemistry, McGill University, Montreal, Quebec, Canada. Electronic address: michel.tremblay@mcgill.ca.
⁶ World Premier International (WPI) Immunology Frontier Research Center (IFReC), Osaka University, 3-1 Yamadaoka, Suita 565-0871, Osaka, Japan; Centro de Biología Molecular Severo Ochoa, CSIC/Universidad Autónoma de Madrid, 28049 Madrid, Spain; IE Business School, IE University, María de Molina 31 bis, 28006 Madrid, Spain. Electronic address: diego@ifrec.osaka-u.ac.jp.

PMID: 25771859
DOI: 10.1016/j.febslet.2015.03.005

Abstract

Most of our knowledge on protein tyrosine phosphatases (PTPs) is derived from human pathologies and mouse knockout models. These models largely correlate well with human disease phenotypes, but can be ambiguous due to compensatory mechanisms introduced by paralogous genes. Here we present the analysis of the PTP complement of the fruit fly and the complementary view that PTP studies in Drosophila will accelerate our understanding of PTPs in physiological and pathological conditions. With only 44 PTP genes, Drosophila represents a streamlined version of the human complement. Our integrated analysis places the Drosophila PTPs into evolutionary and functional contexts, thereby providing a platform for the exploitation of the fly for PTP research and the transfer of knowledge onto other model systems.

Keywords: Biochemical evolution; Drosophila; Model system; PTP-central; Phosphorylation; Sequence analysis; Tyrosine phosphatase.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Animals
Drosophila Proteins / classification
Drosophila Proteins / genetics*
Drosophila Proteins / metabolism
Drosophila melanogaster / enzymology
Drosophila melanogaster / genetics*
Evolution, Molecular
Humans
Mice
Multigene Family*
Mutation
Phylogeny
Protein Tyrosine Phosphatases / classification
Protein Tyrosine Phosphatases / genetics*
Protein Tyrosine Phosphatases / metabolism

Substances

Drosophila Proteins
Protein Tyrosine Phosphatases