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

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          Abstract

          hGAAP promotes cell adhesion and migration by increasing localized Ca 2+-dependent activation of calpain, leading to increased focal adhesion dynamics.

          Abstract

          Golgi antiapoptotic proteins (GAAPs) are highly conserved Golgi membrane proteins that inhibit apoptosis and promote Ca 2+ release from intracellular stores. Given the role of Ca 2+ 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 Ca 2+ 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 Ca 2+-dependent activation of calpain.

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          Disruption of epithelial cell-matrix interactions induces apoptosis

          S. Francis, SM Frisch (1994)
          Cell-matrix interactions have major effects upon phenotypic features such as gene regulation, cytoskeletal structure, differentiation, and aspects of cell growth control. Programmed cell death (apoptosis) is crucial for maintaining appropriate cell number and tissue organization. It was therefore of interest to determine whether cell- matrix interactions affect apoptosis. The present report demonstrates that apoptosis was induced by disruption of the interactions between normal epithelial cells and extracellular matrix. We have termed this phenomenon "anoikis." Overexpression of bcl-2 protected cells against anoikis. Cellular sensitivity to anoikis was apparently regulated: (a) anoikis did not occur in normal fibroblasts; (b) it was abrogated in epithelial cells by transformation with v-Ha-ras, v-src, or treatment with phorbol ester; (c) sensitivity to anoikis was conferred upon HT1080 cells or v-Ha-ras-transformed MDCK cells by reverse- transformation with adenovirus E1a; (d) anoikis in MDCK cells was alleviated by the motility factor, scatter factor. The results suggest that the circumvention of anoikis accompanies the acquisition of anchorage independence or cell motility.
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            Integrin-regulated FAK-Src signaling in normal and cancer cells.

            Satyajit K. Mitra, David Schlaepfer (2006)
            Integrins can alter cellular behavior through the recruitment and activation of signaling proteins such as non-receptor tyrosine kinases including focal adhesion kinase (FAK) and c-Src that form a dual kinase complex. The FAK-Src complex binds to and can phosphorylate various adaptor proteins such as p130Cas and paxillin. In normal cells, multiple integrin-regulated linkages exist to activate FAK or Src. Activated FAK-Src functions to promote cell motility, cell cycle progression and cell survival. Recent studies have found that the FAK-Src complex is activated in many tumor cells and generates signals leading to tumor growth and metastasis. As both FAK and Src catalytic activities are important in promoting VEGF-associated tumor angiogenesis and protease-associated tumor metastasis, support is growing that FAK and Src may be therapeutically relevant targets in the inhibition of tumor progression.
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              FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly.

              Donna J Webb, Karen Donais, Leanna Whitmore … (2004)
              Cell migration is a complex, highly regulated process that involves the continuous formation and disassembly of adhesions (adhesion turnover). Adhesion formation takes place at the leading edge of protrusions, whereas disassembly occurs both at the cell rear and at the base of protrusions. Despite the importance of these processes in migration, the mechanisms that regulate adhesion formation and disassembly remain largely unknown. Here we develop quantitative assays to measure the rate of incorporation of molecules into adhesions and the departure of these proteins from adhesions. Using these assays, we show that kinases and adaptor molecules, including focal adhesion kinase (FAK), Src, p130CAS, paxillin, extracellular signal-regulated kinase (ERK) and myosin light-chain kinase (MLCK) are critical for adhesion turnover at the cell front, a process central to migration.
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Cell Biol
                Journal ID (iso-abbrev): J. Cell Biol
                Journal ID (hwp): jcb
                Title: The Journal of Cell Biology
                Publisher: The Rockefeller University Press
                ISSN (Print): 0021-9525
                ISSN (Electronic): 1540-8140
                Publication date (Print): 19 August 2013
                Volume: 202
                Issue: 4
                Pages: 699-713
                Affiliations
                [1 ]Department of Pathology and [2 ]Department of Pharmacology, University of Cambridge, Cambridge CB2 1QP, England, UK
                [3 ]Section of Virology, Department of Medicine, Imperial College London, London W2 1PG, England, UK
                [4 ]Randall Division of Cell and Molecular Biophysics, King’s College London, London SE1 1UL, England, UK
                Author notes
                Correspondence to Geoffrey L. Smith: gls37@ 123456cam.ac.uk ; or Maddy Parsons: maddy.parsons@ 123456kcl.ac.uk

                D.L. Prole and G. Carrara contributed equally to this paper.

                Article
                Publisher ID: 201301016
                DOI: 10.1083/jcb.201301016
                PMC ID: 3747308
                PubMed ID: 23940116
                SO-VID: 0b19bf19-e621-49af-94ee-bbe979551df5
                Copyright © © 2013 Saraiva et al.
                License:

                This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

                History
                Date received : 4 January 2013
                Date accepted : 11 July 2013
                Categories
                Subject: Research Articles
                Subject: Article

                ScienceOpen disciplines: Cell biology
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                ScienceOpen disciplines: Cell biology

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