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ERK1/2 MAP kinases promote cell cycle entry by rapid, kinase-independent disruption of Retinoblastoma–LaminA complexes.ERK1/2 MAP kinases promote cell cycle entry by rapid, kinase-independent disruption of Retinoblastoma–LaminA complexes.Rodríguez J., Calvo F., González J.M., Casar B., Andrés V. and Crespo P. J. Cell Biol. 191, 967-979. (2010). (Editorial en el mismo número; Editorial en Science Sig. 3, ec371 2010; Seleccionado por The Faculty of 1000).2010-06-04T22:00:00Z<p style="text-align:justify;"><span class="ms-rteThemeForeColor-2-5"><strong>​</strong><span class="ms-rteThemeFontFace-1 ms-rteFontSize-2"><strong>Abstract</strong></span></span></p><p style="text-align:justify;"><span class="ms-rteThemeFontFace-1 ms-rteFontSize-2"><span style="color:#985735;"></span><span style="color:#000000;">As orchestrators of essential cellular processes like proliferation, ERK1/2 mitogen-activated protein kinase signals impact on cell cycle regulation. A-type lamins are major constituents of the nuclear matrix that also control the cell cycle machinery by largely unknown mechanisms. In this paper, we disclose a functional liaison between ERK1/2 and lamin A whereby cell cycle progression is regulated. We demonstrate that lamin A serves as a mutually exclusive dock for ERK1/2 and the retinoblastoma (Rb) protein. Our results reveal that, immediately after their postactivation entrance in the nucleus, ERK1/2 dislodge Rb from its interaction with lamin A, thereby facilitating its rapid phosphorylation and consequently promoting E2F activation and cell cycle entry. Interestingly, these effects are independent of ERK1/2 kinase activity. We also show that cellular transformation and tumor cell proliferation are dependent on the balance between lamin A and nuclear ERK1/2 levels, which determines Rb accessibility for phosphorylation/inactivation.</span></span></p><p><span class="ms-rteForeColor-2"><a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2995174/">​[pubmed]</a></span></p>61