14-3-3 Binding to Cyclin Y contributes to cyclin Y/CDK14 association

Li, Shan; Jiang, Mei; Wang, Wenjuan; Chen, Jiangye

doi:10.1093/abbs/gmu005

Cited by 14 publications

(10 citation statements)

References 24 publications

(27 reference statements)

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“…To our knowledge, the present study is the first study demonstrating that the interaction between PCTAIRE-1 and cyclin Y requires phosphorylation of cyclin Y that results in 14-3-3 binding. However, it should be noted that a recent study by Li et al [ 21 ] has reported cyclin Y binding of 14-3-3, which was associated with interaction with a closely related kinase of PCTAIRE-1, namely PFTAIRE-1/CDK14. They showed that the S100A/S326A double mutant of cyclin Y failed to interact with 14-3-3 and PFTAIRE-1/CDK14.…”

Section: Discussionmentioning

confidence: 98%

Cyclin Y phosphorylation- and 14-3-3-binding-dependent activation of PCTAIRE-1/CDK16

Shehata

Deák

Morrice

et al. 2015

Biochemical Journal

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Section: Discussionmentioning

confidence: 98%

Cyclin Y phosphorylation- and 14-3-3-binding-dependent activation of PCTAIRE-1/CDK16

Shehata

Deák

Morrice

et al. 2015

Biochemical Journal

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“…This sequence is important for CDK16 association with its cognate cyclin, cyclin Y or cyclin Y-like 1 [ 3 , 41 – 43 ]. In addition, stable association of cyclin Y with either CDK14 [ 44 ] or CDK16 [ 45 ] requires cyclin Y phosphorylation and binding to 14-3-3, suggesting that a classical bidentate 14-3-3–ligand interaction [ 46 ] may help to organize cyclin Y to bind to its cognate CDK partner.…”

Section: Relating Structure and Functionmentioning

confidence: 99%

Structural insights into the functional diversity of the CDK–cyclin family

Wood¹,

Endicott²

2018

Open Biol.

187

162

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Since their characterization as conserved modules that regulate progression through the eukaryotic cell cycle, cyclin-dependent protein kinases (CDKs) in higher eukaryotic cells are now also emerging as significant regulators of transcription, metabolism and cell differentiation. The cyclins, though originally characterized as CDK partners, also have CDK-independent roles that include the regulation of DNA damage repair and transcriptional programmes that direct cell differentiation, apoptosis and metabolic flux. This review compares the structures of the members of the CDK and cyclin families determined by X-ray crystallography, and considers what mechanistic insights they provide to guide functional studies and distinguish CDK- and cyclin-specific activities. Aberrant CDK activity is a hallmark of a number of diseases, and structural studies can provide important insights to identify novel routes to therapy.

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“…Cyclin Y/CDK14 participates in the activation of the Wnt signaling pathway particularly in the G 2 /M-phase, consistent with differential expression pattern of CDK14 during the cell cycle, while CDK16 is present throughout the cell cycle 30,37 . Interestingly, the interaction of CDK14 with Cyclin Y has also been proposed to depend on S326 phosphorylation 38 . For CDK15 no functional data are available.…”

Section: Articlementioning

confidence: 99%

AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy

et al. 2020

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The AMP-activated protein kinase (AMPK) is a master sensor of the cellular energy status that is crucial for the adaptive response to limited energy availability. AMPK is implicated in the regulation of many cellular processes, including autophagy. However, the precise mechanisms by which AMPK controls these processes and the identities of relevant substrates are not fully understood. Using protein microarrays, we identify Cyclin Y as an AMPK substrate that is phosphorylated at Serine 326 (S326) both in vitro and in cells. Phosphorylation of Cyclin Y at S326 promotes its interaction with the Cyclin-dependent kinase 16 (CDK16), thereby stimulating its catalytic activity. When expressed in cells, Cyclin Y/CDK16 is sufficient to promote autophagy. Moreover, Cyclin Y/CDK16 is necessary for efficient AMPK-dependent activation of autophagy. This functional interaction is mediated by AMPK phosphorylating S326 of Cyclin Y. Collectively, we define Cyclin Y/CDK16 as downstream effector of AMPK for inducing autophagy.

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14-3-3 Binding to Cyclin Y contributes to cyclin Y/CDK14 association

Cited by 14 publications

References 24 publications

Cyclin Y phosphorylation- and 14-3-3-binding-dependent activation of PCTAIRE-1/CDK16

Cyclin Y phosphorylation- and 14-3-3-binding-dependent activation of PCTAIRE-1/CDK16

Structural insights into the functional diversity of the CDK–cyclin family

AMPK-dependent activation of the Cyclin Y/CDK16 complex controls autophagy

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