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. 2013 Apr;1830(4):2938-45.
doi: 10.1016/j.bbagen.2012.12.020. Epub 2012 Dec 31.

CK2 phosphorylation of human Sec63 regulates its interaction with Sec62

Emmanuel Ampofo  1 , Sabrina Welker, Martin Jung, Linda Müller, Markus Greiner, Richard Zimmermann, Mathias Montenarh
Affiliations

CK2 phosphorylation of human Sec63 regulates its interaction with Sec62

Emmanuel Ampofo et al. Biochim Biophys Acta. 2013 Apr.

Abstract

Background: Protein kinase CK2 is a pleiotropic enzyme which is ubiquitously expressed in eukaryotic cells. Several years ago CK2 was found to be associated with the mammalian endoplasmic reticulum. So far nothing is known about the function of CK2 at the ER.

Methods: CK2 phosphorylation sites in the polypeptide chain of Sec63 were mapped using deletion mutants and a peptide library. Binding of Sec63 to CK2 and to Sec62 was analyzed by pull-down assays and by co-immunoprecipitation

Results: Sec63 was identified as a novel substrate and binding partner of protein kinase CK2. We identified serine 574, serine 576 and serine 748 as CK2 phosphorylation sites. Phosphorylation of Sec63 by CK2 enhanced its binding to Sec62.

Conclusions: Protein kinase CK2 phosphorylation of Sec63 leads to an enhanced binding of Sec63 to Sec62. This complex formation is a prerequisite for a functional ER protein translocon.

General significance: Thus, our present data indicate a regulatory role of CK2 in the ER protein translocation.

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