This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Giurisato, E.
Right arrow Articles by Shaw, A. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Giurisato, E.
Right arrow Articles by Shaw, A. S.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, March 2009, p. 1554-1564, Vol. 29, No. 6
0270-7306/09/$08.00+0     doi:10.1128/MCB.01421-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Mitogen-Activated Protein Kinase Scaffold KSR1 Is Required for Recruitment of Extracellular Signal-Regulated Kinase to the Immunological Synapse{triangledown}

Emanuele Giurisato,1 Joseph Lin,1 Angus Harding,1,{dagger} Elisa Cerutti,1 Marina Cella,1 Robert E. Lewis,2 Marco Colonna,1 and Andrey S. Shaw1,3*

Department of Pathology & Immunology, Washington University School of Medicine, St. Louis, Missouri 63110,1 Department of Pathology, University of Nebraska Medical Center, Eppley Cancer Institute, Omaha, Nebraska 68198-7696,2 Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, Missouri 631103

Received 10 September 2008/ Returned for modification 8 October 2008/ Accepted 19 December 2008

KSR1 is a mitogen-activated protein (MAP) kinase scaffold that enhances the activation of the MAP kinase extracellular signal-regulated kinase (ERK). The function of KSR1 in NK cell function is not known. Here we show that KSR1 is required for efficient NK-mediated cytolysis and polarization of cytolytic granules. Single-cell analysis showed that ERK is activated in an all-or-none fashion in both wild-type and KSR1-deficient cells. In the absence of KSR1, however, the efficiency of ERK activation is attenuated. Imaging studies showed that KSR1 is recruited to the immunological synapse during T-cell activation and that membrane recruitment of KSR1 is required for recruitment of active ERK to the synapse.

* Corresponding author. Mailing address: Department of Pathology & Immunology, Washington University School of Medicine, St. Louis, MO 63110. Phone: (314) 362-6311. Fax: (314) 362-8888. E-mail: shaw{at}pathology.wustl.edu

{triangledown} Published ahead of print on 12 January 2009.

{dagger} Present address: Queensland Brain Institute, University of Queensland, QBI Building 79, St. Lucia, QLD 4072, Australia.

Molecular and Cellular Biology, March 2009, p. 1554-1564, Vol. 29, No. 6
0270-7306/09/$08.00+0     doi:10.1128/MCB.01421-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»