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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAAIUkM4cC0IPkzVmQCVqo7dA-D7dYtNZSqHspMHJ_I_M#_8 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAAIUkM4cC0IPkzVmQCVqo7dA-D7dYtNZSqHspMHJ_I_M#_7 http://www.w3.org/ns/prov#value # Ariadne: Apparently all D- type cyclins can block MEF2 activity as cotransfection of cyclin D1, D2, or D3 together with cdk4 blocked the ability of exogenous MEF2C to activate expression of the MEF2x3LUC reporter in 10T1/2 cells (Fig. 1 C, cf. lane 2 with lanes 3,4,5). [Regulation] # Ariadne: In addition, because it is known that GRIP-1 can rapidly exchange in and out of the punctate nuclear structures when bound to steroid hormone receptors ( Schaufele et al. 2000 ), it seems possible that the GRIP-1-MEF2 complex may similarly diffuse in and out of these structures. [Binding] Prior work has indicated that D-type cyclin-cdk4 complexes, which are only active in proliferating cells, can suppress the skeletal muscle differentiation program in proliferating myoblasts. We have found that cyclin D-cdk activity blocks the association of MEF2C with the coactivator protein GRIP-1 and thereby inhibits the activity of MEF2. 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