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JCS ePress
online publication date 27 May 2003
doi: 10.1242/jcs.00480
Research Article
BTG2 antiproliferative protein interacts with the human CCR4 complex existing in vivo in three cell-cycle-regulated forms
Anne-Pierre Morel,
Stéphanie Sentis,
Claire Bianchin,
Muriel Le Romancer,
Laurence Jonard,
Marie-Claude Rostan,
Ruth Rimokh,
and
Laura Corbo*
* Author for correspondence (e-mail: corbo{at}lyon.fnclcc.fr)
The yeast CCR4-NOT complex exists in two forms (1.0 and 1.9 MDa) that share several common subunits, including yCCR4, yCAF1 and five NOT proteins (NOT1-5). Here, we report that different complexes containing mammalian homologs of CCR4-NOT subunits exist in mammalian cells, with estimated sizes of 
1.9 MDa, 1 MDa and 650 kDa, and that BTG2, a member of a protein family with antiproliferative functions, can associate with these complexes. Immunoprecipitation and gel filtration experiments established that BTG2 interacts in vivo with hCCR4 protein via hCAF1 and hPOP2. Moreover, we show that hCCR4, as well as hCAF1 and BTG2, modulate the transcription regulation mediated by ER
. Finally, we demonstrate that the cellular localization of hCAF1 and the cell content in hCAF1-containing complexes change as cells progress from quiescence to S phase. These findings suggest that the different regulatory pathways in which hCAF1 is involved, notably transcription regulation and mRNA turnover, may occur through distinct CCR4 complexes in the course of cell-cycle progression.
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