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CDK15 — E2F1

Text-mined interactions from Literome

Wu et al., Nature 2001 : Loss of E2F function results in an elevation of p21Cip1 protein, leading to a decrease in cyclin dependent kinase activity and Rb phosphorylation
Hirao et al., Carcinogenesis 2002 (Mesothelioma...) : The p16(INK4a) protein, by inhibiting cyclin dependent kinase , down regulates Rb-E2F and leads to cell cycle arrest in the G1 phase
DeGregori et al., Genes Dev 1995 : We now demonstrate that G1 cyclin dependent kinase activity is critical for the accumulation of E2F activity late in G1
Khleif et al., Proc Natl Acad Sci U S A 1996 (Uterine Cervical Neoplasms) : We conclude that the accumulation of G1 cyclin dependent kinase activity during normal G1 progression leads to E2F accumulation through the inactivation of RB, and that this then leads to the induction of cyclin kinase inhibitor activity and a shutdown of G1 kinase activity
Flink et al., J Mol Cell Cardiol 1998 : Changes in E2F complexes containing retinoblastoma protein family members and increased cyclin dependent kinase inhibitor activities during terminal differentiation of cardiomyocytes
Kohn et al., Oncogene 1998 : The results suggested new functional concepts : ( 1 ) Rb-family proteins could store E2F in a manner analogous to the way a condenser stores electric charge, and, upon phosphorylation, release a large wave of active E2F; (2) excessive or premature cyclin dependent kinase activities could paradoxically impair E2F activity during the G1/S transition period
Gjoerup et al., J Biol Chem 1998 (Genetic Predisposition to Disease) : The inhibitory effect of the cyclin dependent kinase inhibitors, p16(ink4), p21 ( cip1 ), and p27 ( cip ) on Rac/Cdc42 mediated E2F transcription corroborates a role for pRB family members and their functional inactivation by cyclin dependent kinases in generating E2F activity
Garriga et al., Biochem J 1998 (Glioblastoma) : Thus in addition to the direct disruption of pocket protein/E2F complexes induced by cyclin/cyclin dependent kinase , the results we report here indicate that the differential modulation of pocket protein levels constitutes a major mechanism that regulates the pool of each pocket protein that is accessible to E2F and/or other transcription factors