Cell
ArticleCell cycle regulation of the E2F transcription factor involves an interaction with cyclin A
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Multiple domains in the 50 kDa form of E4F1 regulate promoter-specific repression and E1A trans-activation
2020, GeneCitation Excerpt :The identities of the specific cellular activities involved in this mechanism await further investigation. However, given that this mechanism involves the stimulation of phosphorylation within the DNA binding domain, it is reasonable to speculate that this involves one or more of the multiple cellular kinase and/or phosphatase activities that are known to associate with or are regulated by E1A289R and E1A243R (Mudryj et al., 1991; Wang et al., 1991; Herrmann et al., 1991; Kleinberger and Shenk, 1991; Dyson and Harlow, 1992; Peeper and Zantema, 1993; Barbeau et al., 1994; Dyson, 1998; Herrmann et al., 1996; Shao et al., 1999; Parreño et al., 2001; Liao and Hung, 2003; Liao and Hung, 2004; Guan et al., 2008; Callejas-Valera et al., 2008). The E1A289R CR3-dependent mechanism revealed in this report involves a previously described transcription regulatory region in p50E4F1 (Fernandes and Rooney, 1999).
Cyclin F Controls Cell-Cycle Transcriptional Outputs by Directing the Degradation of the Three Activator E2Fs
2019, Molecular CellCitation Excerpt :At the end of the S phase, E2F-mediated transcription is turned off through negative feedback loops and the subsequent activation of atypical repressors (Li et al., 2008a; Westendorp et al., 2012). Two major components of the negative feedback, cyclin A2 and CDK2 (the products of two E2F target genes), form an active kinase complex that phosphorylates E2F1 and inhibits its transcription activity (Dynlacht et al., 1994; Krek et al., 1994; Mudryj et al., 1991; Pagano et al., 1992). Moreover, the F box protein SKP2 has been suggested to promote the degradation of E2F1 in S and G2 (Marti et al., 1999).
The nuclear protein UHRF2 is a direct target of the transcription factor E2F1 in the induction of apoptosis
2013, Journal of Biological ChemistryCitation Excerpt :CCNA2 (cyclin A2) is a member of the conserved cyclin family of proteins that binds to and controls cyclin-dependent kinases and function as regulators of G1/S and G2/M cell cycle transitions. Interestingly, CCNA2-CDK2 complexes bind to and phosphorylate the amino terminus of E2F1, inhibiting its DNA binding affinity (28, 29). AZIN1 (antizyme inhibitor 1) indirectly regulate polyamine biosynthesis through the stabilization of ornithine decarboxylase, a mediator of the ornithine to putrescine conversion (30).
Impact of cell cycle disruption on impaired hepatic regeneration in aged livers with ischemic insult
2012, Journal of Surgical ResearchErk1/2 promotes proliferation and inhibits neuronal differentiation of neural stem cells
2009, Neuroscience LettersDirect association of the HPV16 E7 oncoprotein with cyclin A/CDK2 and cyclin E/CDK2 complexes
2008, VirologyCitation Excerpt :Moreover, because cyclin/CDK2 complexes play important roles in the cell cycle and an essential activity of HPV16 E7 is the disruption of the cell cycle to achieve S-phase competence, it was important to more clearly dissect the nature of the interplay between HPV E7 proteins and cyclin/CDK2 complexes. Similar to the subcellular localization of HPV16 E7, while cyclin E/CDK2 and cyclin A/CDK2 are critical components of nuclear pRB family member containing E2F transcription factor complexes (Devoto et al., 1992; Lees et al., 1992; Mudryj et al., 1991; Shirodkar et al., 1992), which HPV16 E7 is known to bind (Arroyo et al., 1993), CDK2 has also been detected in the cytoplasm and on centrosomes (Jackman et al., 2002). Therefore, HPV16 E7 would be capable of associating with cyclin/CDK2 complexes both in the nucleus, where pRB is present, as well as in the cytoplasm.