Cell-surface-associated proteolysis plays a crucial role in embryonic development, monocyte/macrophage recruitment and tumour cell invasion. The glycolytic enzyme ENO-1 (enolase-1) is translocated from the cytoplasm to the cell surface, where it binds PLG (plasminogen) to enhance pericellular plasmin production and cell motility. In the present study, ENO-1 was found to localize to a specialized subset of lipid rafts called caveolae as demonstrated by fluorescence confocal microscopy and sucrose gradient ultracentrifugation. Co-immunoprecipitation studies revealed that ENO-1 interacts with Cav-1 (caveolin-1), but not with Cav-2, via the CSD (Cav-scaffolding domain). Moreover, an evolutionarily conserved CBM (Cav-binding motif) F296DQDDWGAW304 was identified within ENO-1. The point mutation W301A within the ENO-1 CBM was, however, not sufficient to disrupt ENO-1–Cav-1 interaction, whereas the mutations F296A and W304A markedly affected ENO-1 protein expression. Furthermore, ENO-1 was found associated with Annx2 (annexin 2), representing another caveolar protein, and this interaction was dependent on Cav-1 expression. Knockdown of Cav-1 and Annx2 markedly decreased cell surface expression of ENO-1. ENO-1 overexpression increased cell migration and invasion in a Cav-1-dependent manner. Thus the differential association of ENO-1 with caveolar proteins regulates ENO-1 subcellular localization and, consequently, ENO-1-dependent cell migration and invasion.
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Research Article|
May 13 2014
The interaction of enolase-1 with caveolae-associated proteins regulates its subcellular localization
Dariusz Zakrzewicz;
Dariusz Zakrzewicz
1
*Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany
1To whom correspondence should be addressed (email dariusz.zakrzewicz@innere.med.uni-giessen.de).
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Miroslava Didiasova;
Miroslava Didiasova
*Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany
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Anna Zakrzewicz;
Anna Zakrzewicz
†Laboratory of Experimental Surgery, Department of General and Thoracic Surgery, Justus Liebig-University Giessen, Feulgenstrasse 10-12, 35385 Giessen, Germany
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Andreas C. Hocke;
Andreas C. Hocke
‡Department of Internal Medicine/Infectious Diseases and Pulmonary Medicine, Charité-University Medicine Berlin, Chariteplatz 1, 10117 Berlin, Germany
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Florian Uhle;
Florian Uhle
§Departments of Anaesthesiology and Operative Intensive Care, University Hospital Giessen and Marburg GmbH, Klinikstrasse 33, Giessen 35392, Germany
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Philipp Markart;
Philipp Markart
∥Department of Internal Medicine, University Hospital Giessen and Marburg GmbH, Klinikstrasse 33, Giessen 35392, Germany
¶Member of the German Center for Lung Research, Giessen, Germany
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Klaus T. Preissner;
Klaus T. Preissner
*Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany
¶Member of the German Center for Lung Research, Giessen, Germany
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Malgorzata Wygrecka
Malgorzata Wygrecka
*Department of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany
¶Member of the German Center for Lung Research, Giessen, Germany
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Publisher: Portland Press Ltd
Received:
July 17 2013
Revision Received:
February 10 2014
Accepted:
March 14 2014
Accepted Manuscript online:
March 14 2014
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem J (2014) 460 (2): 295–307.
Article history
Received:
July 17 2013
Revision Received:
February 10 2014
Accepted:
March 14 2014
Accepted Manuscript online:
March 14 2014
Citation
Dariusz Zakrzewicz, Miroslava Didiasova, Anna Zakrzewicz, Andreas C. Hocke, Florian Uhle, Philipp Markart, Klaus T. Preissner, Malgorzata Wygrecka; The interaction of enolase-1 with caveolae-associated proteins regulates its subcellular localization. Biochem J 1 June 2014; 460 (2): 295–307. doi: https://doi.org/10.1042/BJ20130945
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