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Published 3 September 2001. doi:10.1083/jcb.200105121
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© 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


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