Evidence that phosphorylation by the mitotic kinase Cdk1 promotes ICER monoubiquitination and nuclear delocalization

Elisabeth Mémin, Megan Genzale, Marni Crow, Carlos Molina

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

In contrast to normal prostatic cells, the transcriptional repressor Inducible cAMP Early Repressor (ICER) is undetected in the nuclei of prostate cancer cells. The molecular mechanisms for ICER abnormal expression in prostate cancer cells remained largely unknown. In this report data is presented demonstrating that ICER is phosphorylated by the mitotic kinase cdk1. Phosphorylation of ICER on a discrete residue targeted ICER to be monoubiquitinated. Different from unphosphorylated, phosphorylated and polyubiquitinated ICER, monoubiquitinated ICER was found to be cytosolic. Taken together, these results hinted on a mechanism for the observed abnormal subcellular localization of ICER in human prostate tumors.

Original languageEnglish
Pages (from-to)2490-2502
Number of pages13
JournalExperimental Cell Research
Volume317
Issue number17
DOIs
StatePublished - 1 Jan 2011

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CDC2 Protein Kinase
Phosphorylation
Prostatic Neoplasms
Prostate
Neoplasms

Keywords

  • Cdk1
  • ICER
  • Phosphorylation
  • Ubiquitination

Cite this

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abstract = "In contrast to normal prostatic cells, the transcriptional repressor Inducible cAMP Early Repressor (ICER) is undetected in the nuclei of prostate cancer cells. The molecular mechanisms for ICER abnormal expression in prostate cancer cells remained largely unknown. In this report data is presented demonstrating that ICER is phosphorylated by the mitotic kinase cdk1. Phosphorylation of ICER on a discrete residue targeted ICER to be monoubiquitinated. Different from unphosphorylated, phosphorylated and polyubiquitinated ICER, monoubiquitinated ICER was found to be cytosolic. Taken together, these results hinted on a mechanism for the observed abnormal subcellular localization of ICER in human prostate tumors.",
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Evidence that phosphorylation by the mitotic kinase Cdk1 promotes ICER monoubiquitination and nuclear delocalization. / Mémin, Elisabeth; Genzale, Megan; Crow, Marni; Molina, Carlos.

In: Experimental Cell Research, Vol. 317, No. 17, 01.01.2011, p. 2490-2502.

Research output: Contribution to journalArticle

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