JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 3 September 2001. doi:10.1083/jcb.200105121
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 395K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sussman, J.
Right arrow Articles by Shtivelman, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sussman, J.
Right arrow Articles by Shtivelman, E.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0021-9525/2001/9/1019 $5.00
The Journal of Cell Biology, Volume 154, Number 5, September 3, 2001 1019-1030

Article

 Protein kinase B phosphorylates AHNAK and regulates its subcellular localization

Joshua Sussman, David Stokoe, Natalya Ossina and Emma Shtivelman

Cancer Research Institute, University of California at San Francisco, San Francisco, CA 94143

Address correspondence to Emma Shtivelman, Cancer Research Institute, University of California at San Francisco, 2340 Sutter St., San Francisco, CA 94143. Tel.: (415) 502-1985. Fax: (415) 502-3179. E-mail: shtivelman{at}cc.uscf.edu

AHNAK is a ubiquitously expressed giant phosphoprotein that was initially identified as a gene product subject to transcriptional repression in neuroblastoma. AHNAK is predominantly nuclear in cells of nonepithelial origin, but is cytoplasmic or associated with plasma membrane in epithelial cells. In this study we show that the extranuclear localization of AHNAK in epithelial cells depends on the formation of cell–cell contacts. We show that AHNAK is a phosphorylation substrate of protein kinase B (PKB) in vitro and in vivo. Nuclear exclusion of AHNAK is mediated through a nuclear export signal (NES) in a manner that depends on the phosphorylation of serine 5535 of AHNAK by PKB, a process that also plays a major role in determining extranuclear localization of AHNAK. AHNAK is a new PKB substrate whose function, though unknown, is likely to be regulated by its localization, which is in turn regulated by PKB.

Key Words: AHNAK; PKB; nuclear export; leptomycin B; cell–cell contacts


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents