Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

Comparative analysis of the Band 4.1/ezrin-related protein tyrosine phosphatase Pez from two Drosophila species: implications for structure and function

Edwards, Kevin, Davis, Terence, Marcey, David, Kurihara, Joyce and Yamamoto, Daisuke 2001. Comparative analysis of the Band 4.1/ezrin-related protein tyrosine phosphatase Pez from two Drosophila species: implications for structure and function. Gene 275 (2) , pp. 195-205. 10.1016/S0378-1119(01)00686-2

Full text not available from this repository.

Abstract

The FERM-PTPs are a group of proteins that have FERM (Band 4.1, ezrin, radixin, moesin homology) domains at or near their N-termini, and PTP (protein tyrosine phosphatase) domains at their C-termini. Their central regions contain either PSD-95, Dlg, ZO-1 homology domains or putative Src homology 3 domain binding sites. The known FERM-PTPs fall into three distinct classes, which we name BAS, MEG, and PEZ, after representative human PTPs. Here we analyze Pez, a novel gene encoding the single PEZ-class protein present in Drosophila. Pez cDNAs were sequenced from the distantly related flies Drosophila melanogaster and Drosophila silvestris, and found to be highly conserved except in the central region, which contains at least 21 insertions and deletions. Comparison of fly and human Pez reveals several short conserved motifs in the central region that are likely protein binding sites and/or phosphorylation sites. We also identified novel invertebrate members of the BAS and MEG classes using genome data, and generated an alignment of vertebrate and invertebrate FERM domains of each class. ‘Specialized’ residues were identified that are conserved only within a given class of PTPs. These residues highlight surface regions that may bind class-specific ligands; for PEZ, these residues cluster on and near FERM subdomain F1. Finally, the PTP domain of fly Pez was modeled based on known PTP tertiary structures, and we conclude that Pez is likely a functional phosphatase despite some unusual features of the active site cleft sequences. Biochemical confirmation of this hypothesis and genetic analysis of Pez are currently underway.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: Q Science > QH Natural history > QH426 Genetics
R Medicine > R Medicine (General)
Uncontrolled Keywords: Drosophila melanogaster; Drosophila silvestris; FERM domain; PTP36/PTPD1; PTP-MEG1/PTPH1
Publisher: Elsevier
ISSN: 0378-1119
Last Modified: 04 Jun 2017 06:40
URI: http://orca-mwe.cf.ac.uk/id/eprint/63561

Actions (repository staff only)

Edit Item Edit Item