The kinesin I family member KIF5C is a novel substrate for protein kinase CK2
- Medizinische Biochemie und Molekularbiologie, Universitaet des Saarlandes, Gebaeude 44, 66424 Homburg (Germany)
Protein kinase CK2 is ubiquitously expressed. The holoenzyme is composed of two catalytic {alpha}- or {alpha}'-subunits and two regulatory {beta}-subunits but evidence is accumulating that the subunits can function independently. The composition of the holoenzyme as well as the expression of the individual subunits varies in different tissues, with high expression of CK2{alpha}' in testis and brain. CK2 phosphorylates a number of different substrates which are implicated in basal cellular processes such as proliferation and survival of cells. Here, we report a new substrate, KIF5C, which is a member of the kinesin 1 family of motor neuron proteins. Phosphorylation of KIF5C was demonstrated in vitro and in vivo. Using deletion mutants, a peptide library, and mutation analysis a phosphorylation site for CK2 was mapped to amino acid 338 which is located in the non-motor domain of KIF5C. Interestingly, KIF5C is phosphorylated by holoenzymes composed of CK2{alpha}/CK2{beta} and CK2{alpha}'/CK2{beta} as well as by CK2{alpha}' alone but not by CK2{alpha} alone.
- OSTI ID:
- 21143898
- Journal Information:
- Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 375; ISSN BBRCA9; ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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