Please use this identifier to cite or link to this item:
Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: Ser(756) of β2 integrin controls Rap1 activity during inside-out activation of αMβ2
Author(s): Lim, Jenson
Hotchin, Neil A
Caron, Emmanuelle
Contact Email:
Keywords: αMβ2
calcium/calmodulin-dependent kinase II (CaMKII)
Issue Date: 2011
Date Deposited: 17-Sep-2014
Citation: Lim J, Hotchin NA & Caron E (2011) Ser(756) of β2 integrin controls Rap1 activity during inside-out activation of αMβ2. Biochemical Journal, 437 (3), pp. 461-467.
Abstract: 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.
DOI Link: 10.1042/BJ20101666
Rights: The publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study.
Licence URL(s):

Files in This Item:
File Description SizeFormat 
Lim et al 2011.pdfFulltext - Published Version405.56 kBAdobe PDFUnder Embargo until 3000-12-01    Request a copy

Note: If any of the files in this item are currently embargoed, you can request a copy directly from the author by clicking the padlock icon above. However, this facility is dependent on the depositor still being contactable at their original email address.

This item is protected by original copyright

Items in the Repository are protected by copyright, with all rights reserved, unless otherwise indicated.

The metadata of the records in the Repository are available under the CC0 public domain dedication: No Rights Reserved

If you believe that any material held in STORRE infringes copyright, please contact providing details and we will remove the Work from public display in STORRE and investigate your claim.