Protein kinase B phosphorylates AHNAK and regulates its subcellular localization
| Autor: | Emma Shtivelman, David Stokoe, Joshua Sussman, Natalya Ossina |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Proto-Oncogene Proteins c-akt
Morpholines Recombinant Fusion Proteins Immunoblotting Molecular Sequence Data Active Transport Cell Nucleus Cell Count Protein Serine-Threonine Kinases Protein Sorting Signals Biology Cell Fractionation Article Cell Line Genes Reporter Proto-Oncogene Proteins medicine Humans Amino Acid Sequence Enzyme Inhibitors Phosphorylation Nuclear export signal Protein kinase B Cell Nucleus AHNAK PKB nuclear export leptomycin B cell–cell contacts Membrane Proteins Cell Biology Subcellular localization Neoplasm Proteins Protein Structure Tertiary Cell biology Cell nucleus medicine.anatomical_structure Microscopy Fluorescence Membrane protein Chromones Phosphoprotein |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|