During αMβ2-mediated phagocytosis, the small GTPase Rap1 activates the β2 integrin by binding to a region between residues 732 and 761. Using COS-7 cells transfected with αMβ2, we show that αMβ2 activation by the phorbol ester PMA involves Ser756 of β2. This residue is critical for the local positioning of talin and biochemically interacts with Rap1. Using the CaM (calmodulin) antagonist W7, we found Rap1 recruitment and the inside-out activation of αMβ2 to be affected. We also report a role for CaMKII (calcium/CaM-dependent kinase II) in the activation of Rap1 during integrin activation. These results demonstrate a distinct physiological role for Ser756 of β2 integrin, in conjunction with the actions of talin and Rap1, during αMβ2 activation in macrophages.
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Research Article|
July 13 2011
Ser756 of β2 integrin controls Rap1 activity during inside-out activation of αMβ2
Jenson Lim;
Jenson Lim
1
*Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, U.K.
1To whom correspondence should be addressed (email jensons_blog@yahoo.co.uk).
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Neil A. Hotchin;
Neil A. Hotchin
†School of Biosciences, University of Birmingham, Birmingham B15 2TT, U.K.
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Emmanuelle Caron
Emmanuelle Caron
2
*Centre for Molecular Microbiology and Infection, Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, U.K.
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Publisher: Portland Press Ltd
Received:
November 16 2010
Revision Received:
May 10 2011
Accepted:
May 24 2011
Accepted Manuscript online:
May 24 2011
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem J (2011) 437 (3): 461–467.
Article history
Received:
November 16 2010
Revision Received:
May 10 2011
Accepted:
May 24 2011
Accepted Manuscript online:
May 24 2011
Citation
Jenson Lim, Neil A. Hotchin, Emmanuelle Caron; Ser756 of β2 integrin controls Rap1 activity during inside-out activation of αMβ2. Biochem J 1 August 2011; 437 (3): 461–467. doi: https://doi.org/10.1042/BJ20101666
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