The human phosphatase interactome: An intricate family portrait

被引：172

作者：

Sacco, Francesca ^{[1
]}

Perfetto, Livia ^{[1
]}

Castagnoli, Luisa ^{[1
]}

Cesareni, Gianni ^{[1
,2
]}

机构：

[1] Univ Roma Tor Vergata, Dept Biol, I-00173 Rome, Italy

[2] Fdn Santa Lucia, Res Inst, Rome, Italy

来源：

FEBS LETTERS | 2012年 / 586卷 / 17期

关键词：

Human phosphatome; Phosphatase family classification; Substrate recognition specificity; PROTEIN-TYROSINE-PHOSPHATASE; GROWTH-FACTOR RECEPTOR; SUBSTRATE-SPECIFICITY; IN-VIVO; POSTTRANSLATIONAL MODIFICATIONS; HUMAN GENOME; KINASES; CANCER; PHOSPHORYLATION; ACTIVATION;

D O I：

10.1016/j.febslet.2012.05.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The concerted activities of kinases and phosphatases modulate the phosphorylation levels of proteins, lipids and carbohydrates in eukaryotic cells. Despite considerable effort, we are still missing a holistic picture representing, at a proteome level, the functional relationships between kinases, phosphatases and their substrates. Here we focus on phosphatases and we review and integrate the available information that helps to place the members of the protein phosphatase super-families into the human protein interaction network. In addition we show how protein interaction domains and motifs, either covalently linked to the phosphatase domain or in regulatory/adaptor subunits, play a prominent role in substrate selection. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2732 / 2739

页数：8

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