Abstract：
:Cyclin D1 encodes the regulatory subunit of a holoenzyme that phosphorylates RB and functions as a collaborative nuclear oncogene. The serine threonine kinase Akt plays a pivotal role in the control of cellular metabolism, survival, and mitogenic signaling. Herein, Akt1-mediated phosphorylation of downstream substrates in the mammary gland is reduced by cyclin D1 genetic deletion and is induced by mammary-gland-targeted cyclin D1 overexpression. Cyclin D1 is associated with Akt1 and augments the rate of onset and maximal cellular Akt1 activity induced by mitogens. Cyclin D1 is identified in a cytoplasmic-membrane-associated pool, and cytoplasmic-membrane-localized cyclin D1-but not nuclear-localized cyclin D1-recapitulates Akt1 transcriptional function. These studies identify a novel extranuclear function of cyclin D1 to enhance proliferative functions via augmenting Akt1 phosphorylation at Ser473.
journal_name
Cell Repjournal_title
Cell reportsauthors
Chen K,Jiao X,Di Rocco A,Shen D,Xu S,Ertel A,Yu Z,Di Sante G,Wang M,Li Z,Pestell TG,Casimiro MC,Skordalakes E,Achilefu S,Pestell RGdoi
10.1016/j.celrep.2020.108151subject
Has Abstractpub_date
2020-09-15 00:00:00pages
108151issue
11issn
2211-1247pii
S2211-1247(20)31140-2journal_volume
32pub_type
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