hGAAP promotes cell adhesion and migration via the stimulation of store-operated Ca2+ entry and calpain 2

被引：41
作者：
Saraiva, Nuno [1 ,3 ]
Prole, David L. [2 ]
Carrara, Guia [1 ,3 ]
Johnson, Benjamin F. [3 ]
Taylor, Colin W. [2 ]
Parsons, Maddy [4 ]
Smith, Geoffrey L. [1 ,3 ]
机构：
[1] Univ Cambridge, Dept Pathol, Cambridge CB2 1QP, England
[2] Univ Cambridge, Dept Pharmacol, Cambridge CB2 1QP, England
[3] Univ London Imperial Coll Sci Technol & Med, Dept Med, Virol Sect, London W2 1PG, England
[4] Kings Coll London, Randall Div Cell & Mol Biophys, London SE1 1UL, England
来源：
JOURNAL OF CELL BIOLOGY | 2013年 / 202卷 / 04期
基金：
英国医学研究理事会; 英国惠康基金;
关键词：
BAX INHIBITOR-1; CALPAIN/CALPASTATIN NETWORK; ENDOPLASMIC-RETICULUM; MEDIATED PROTEOLYSIS; CALCIUM GRADIENTS; GENE-EXPRESSION; VACCINIA VIRUS; DYNAMICS; ACTIVATION; PROTEIN;
D O I：
10.1083/jcb.201301016
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Golgi antiapoptotic proteins (GAAPs) are highly conserved Golgi membrane proteins that inhibit apoptosis and promote Ca2+ release from intracellular stores. Given the role of Ca2+ in controlling cell adhesion and motility, we hypothesized that human GAAP (hGAAP) might influence these events. In this paper, we present evidence that hGAAP increased cell adhesion, spreading, and migration in a manner that depended on the C-terminal domain of hGAAP. We show that hGAAP increased store-operated Ca2+ entry and thereby the activity of calpain at newly forming protrusions. These hGAAP-dependent effects regulated focal adhesion dynamics and cell migration. Indeed, inhibition or knockdown of calpain 2 abrogated the effects of hGAAP on cell spreading and migration. Our data reveal that hGAAP is a novel regulator of focal adhesion dynamics, cell adhesion, and migration by controlling localized Ca2+-dependent activation of calpain.
引用
收藏
页码：699 / 713
页数：15
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