MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Smith, J. J.
Right arrow Articles by Kornbluth, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smith, J. J.
Right arrow Articles by Kornbluth, S.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, March 2002, p. 1412-1423, Vol. 22, No. 5
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.5.1412-1423.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Apoptotic Regulation by the Crk Adapter Protein Mediated by Interactions with Wee1 and Crm1/Exportin

Jesse J. Smith,1 D. Ashley Richardson,1 Jan Kopf,2 Minoru Yoshida,3 Robert E. Hollingsworth,2 and Sally Kornbluth1*

Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710,1 Pathway Discovery, GlaxoSmithKline, Inc., Research Triangle Park, North Carolina 27709,2 and Department of Biotechnology, Graduate School of Agriculture & Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan3

Received 12 June 2001/ Returned for modification 6 August 2001/ Accepted 26 November 2001

The adapter protein Crk contains an SH2 domain and two SH3 domains. Through binding of particular ligands to the SH2 domain and the N-terminal SH3 domain, Crk has been implicated in a number of signaling processes, including regulation of cell growth, cell motility, and apoptosis. We report here that the C-terminal SH3 domain, never shown to bind any specific signaling molecules, contains a binding site for the nuclear export factor Crm1. We find that a mutant Crk protein, deficient in Crm1 binding, promotes apoptosis. Moreover, this nuclear export sequence mutant [NES(-) Crk] interacts strongly, through its SH2 domain, with the nuclear tyrosine kinase, Wee1. Collectively, these data suggest that a nuclear population of Crk bound to Wee1 promotes apoptotic death of mammalian cells.

* Corresponding author. Mailing address: Department of Pharmacology and Cancer Biology, Duke University Medical Center, Box 3813, C370 LSRC, Research Dr., Durham, NC 27710. Phone: (919) 613-8624. Fax: (919) 681-1005. E-mail: kornb001{at}mc.duke.edu.

Molecular and Cellular Biology, March 2002, p. 1412-1423, Vol. 22, No. 5
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.5.1412-1423.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2002 by the American Society for Microbiology. All rights reserved.