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Article

Serine 64 phosphorylation enhances the antiapoptotic function of Mcl-1.

The Journal of biological chemistry - 22 Jun 2007

Kobayashi Shogo, Lee Sun-Hee, Meng Xue W, Mott Justin L, Bronk Steven F, Werneburg Nathan W, Craig Ruth W, Kaufmann Scott H, Gores Gregory J

Abstract excerpt

Mcl-1 is an antiapoptotic Bcl-2 family member that is highly regulated and when dysregulated contributes to cancer. The Mcl-1 protein is phosphorylated at multiple sites in response to different signaling events. Phosphorylations at Thr163 (by ERK) and Ser159 (by glycogen-synthase kinase 3beta) have recently been shown to slow and enhance, respectively, Mcl-1 protein turnover. Phosphorylation is also known to be...

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Identifiers

PMID: 17463001
DOI: 10.1074/jbc.M610010200

Genes

CDK1
CDK2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Serine 64 phosphorylation enhances the antiapoptotic function of Mcl-1.PMID 17463001Read ↗

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