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Translokin (Cep57) interacts with cyclin D1 and prevents its nuclear accumulation in quiescent fibroblasts

AuthorsRuiz-Miró, Maria; Colomina, Neus; Fernández, Rita M. H.; Garí, Eloi; Gallego, Carme ; Aldea, Marti
Cyclin D1
Cell quiescence
Cell cycle
Cell proliferation
Issue Date2011
CitationTraffic 12(5): 549-562 (2011)
AbstractNuclear accumulation of cyclin D1 due to altered trafficking or degradation is thought to contribute directly to neoplastic transformation and growth. Mechanisms of cyclin D1 localization in S phase have been studied in detail, but its control during exit from the cell cycle and quiescence is poorly understood. Here we report that translokin, a microtubule-associated protein, interacts with cyclin D1 and controls its nucleocytoplasmic distribution in quiescent cells. Translokin binds to regions of cyclin D1 also involved in binding to Cdk4, and both Cdk4 and translokin compete for binding to cyclin D1. Accordingly, while the interaction efficiency between cyclin D1 and translokin increases, the level of cyclin D1 in Cdk4 complexes decreases in quiescent cells. Downregulation of translokin levels results in undue nuclear accumulation of cyclin D1 and increased Cdk4-dependent phosphorylation of pRB under quiescence conditions. In turn, overexpression of translokin prevents proper cyclin D1 accumulation in the nucleus of proliferating cells in an interaction-dependent manner. We propose that translokin acts as a key negative regulator in the pathway that drives nuclear import of cyclin D1, thus contributing to prevent pRb inactivation and to maintain cellular quiescence.
Identifiersdoi: 10.1111/j.1600-0854.2011.01176.x
issn: 1398-9219
e-issn: 1600-0854
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