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Molecular and Cellular Biology, April 2007, p. 2431-2441, Vol. 27, No. 7
0270-7306/07/$08.00+0     doi:10.1128/MCB.01479-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Src Family Kinases Directly Regulate JIP1 Module Dynamics and Activation{triangledown}

Deepak Nihalani,1 Hetty Wong,1 Rakesh Verma,1 and Lawrence B. Holzman1,2*

Division of Nephrology, Department of Internal Medicine, University of Michigan School of Medicine, Ann Arbor, Michigan 48109-0676,1 Department of Veterans Affairs, Ann Arbor, Michigan 481052

Received 9 August 2006/ Returned for modification 3 October 2006/ Accepted 9 January 2007

JIP1 is a mammalian scaffold protein that assembles and participates in regulating the dynamics and activation of components of the mixed-lineage kinase-dependent JNK module. Mechanisms governing JIP1-JNK module regulation remain unclear. JIP1 is a multiply phosphorylated protein; for this reason, it was hypothesized that signaling by unidentified protein kinases or phosphatases might determine module function. We find that Src family kinases directly bind and tyrosine phosphorylate JIP1 under basal conditions in several naturally occurring systems and, by doing so, appear to provide a regulated signal that increases the affinity of JIP1 for DLK and maintains the JIP-JNK module in a catalytically inactive state.

* Corresponding author. Mailing address: University of Michigan Medical School, Medical Science Research Building 2, 1150 West Medical Center Drive, Ann Arbor, MI 48109-0676. Phone: (734) 764-3157. Fax: (734) 763-0982. E-mail: lholzman{at}umich.edu.

{triangledown} Published ahead of print on 22 January 2007.

Molecular and Cellular Biology, April 2007, p. 2431-2441, Vol. 27, No. 7
0270-7306/07/$08.00+0     doi:10.1128/MCB.01479-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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