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Phosphorylated Calmodulin Promotes PI3K Activation by Binding to the SH(2) Domains

How calmodulin (CaM) acts in KRAS-driven cancers is a vastly important question. CaM binds to and stimulates PI3Kα/Akt signaling, promoting cell growth and proliferation. Phosphorylation of CaM at Tyr(99) (pY99) enhances PI3Kα activation. PI3Kα is a lipid kinase. It phosphorylates PIP(2) to produce...

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Bibliografische gegevens
Gepubliceerd in:Biophys J
Hoofdauteurs: Zhang, Mingzhen, Jang, Hyunbum, Gaponenko, Vadim, Nussinov, Ruth
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: The Biophysical Society 2017
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC5685777/
https://ncbi.nlm.nih.gov/pubmed/29117520
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2017.09.008
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