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Control of Cyclin B1 localization through regulated binding of the nuclear export factor CRM1

Article Abstract:

Cyclin B/Cdc2 kinase complex activation brings on mitosis in all eukaryotic cells. It has been proposed that Cyclin B1 phosphorylation at the G2/M transition does not allow its interaction with CRM1, which helps nuclear accumulation and reduces nuclear export. It is also proposed that observed cytoplasmic localizing of Cyclin B1 in interphase is reflective of equilibrium between ongoing nuclear import and rapid CRM1-mediated export.

Author: Brennan, Jennifer, Yang, Jing, Kornbluth, Sally, Powers, Maureen A., Bardes, ELaine S.G., Moore, Jonathan D.
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
Research, Analysis, Genetic aspects, Cell cycle, Phosphorylation, DNA binding proteins

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Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor

Article Abstract:

The importin alpha/beta heterodimer transports NLS proteins into the nucleus. Importin alpha acts to bind NLS, and importin beta mediates translocation. RanGTP binds importin beta after translocation, and displaces importin alpha. It is reported that the CAS protein mediates importin alpha re-export, but only binds strongly to importin alpha in the presence of RanGTP.

Author: Kostka, Susanne, Gorlich, Dirk, Kraft, Regine, Kutay, Ulirke, Bischoff, F. Ralf
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
Observations, Proteins, Translocation (Genetics)

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