Journal
JOURNAL OF CELL BIOLOGY
Volume 183, Issue 4, Pages 653-666Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200805049
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Funding
- Spanish Ministry of Science and Innovation-MICINN [SAF2004-03057, SAF2007-6211]
- Red Tematica de Investigacion Cooperativa en Enfermedades Cardiovasculares, Instituto de Salud Carlos III-ISCIII [RD06/0014/0021, RD06/0020/0105]
- MICINN [BFU2005-00777, GEN2003-20239-C06-03]
- LSHC [CT-2006-037731]
- SIMAP [IST-2004-027265]
- Generalitat Valenciana [GVPRE/2008/163]
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Sequestration of c-Fos at the nuclear envelope ( NE) through interaction with A-type lamins suppresses AP-1-dependent transcription. We show here that c-Fos accumulation within the extraction-resistant nuclear fraction (ERNF) and its interaction with lamin A are reduced and enhanced by gain-of and loss-of ERK1/2 activity, respectively. Moreover, hindering ERK1/2-dependent phosphorylation of c-Fos attenuates its release from the ERNF induced by serum and promotes its interaction with lamin A. Accordingly, serum stimulation rapidly releases preexisting c-Fos from the NE via ERK1/2-dependent phosphorylation, leading to a fast activation of AP-1 before de novo c-Fos synthesis. Moreover, lamin A-null cells exhibit increased AP-1 activity and reduced levels of c-Fos phosphorylation. We also find that active ERK1/2 interacts with lamin A and colocalizes with c-Fos and A-type lamins at the NE. Thus, NE-bound ERK1/2 functions as a molecular switch for rapid mitogen-dependent AP-1 activation through phosphorylation-induced release of preexisting c-Fos from its inhibitory interaction with lamin A/C.
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