Abstract:
:We have shown previously that the activity of the long myosin light chain kinase (MLCK) is cell cycle regulated with a decrease in specific activity during mitosis that can be restored following treatment with alkaline phosphatase. To better understand the role and significance of phosphorylation in regulating MLCK function during mitosis, we examined the phosphorylation state of in vivo derived MLCK. Phosphoamino acid analysis and phosphopeptide mapping demonstrate that the long MLCK is differentially phosphorylated on serine residues during interphase and mitosis with the majority of the phosphorylation sites located within the N-terminal IgG domain. Biochemical assays show that Aurora B binds and phosphorylates the IgG domain of the long MLCK. In addition, phosphopeptide maps of the endogenous full-length MLCK from mitotic cells and in vitro phosphorylated IgG domain demonstrate that Aurora B phosphorylates the same sites as those observed in vivo. Altogether, these studies suggest that the long MLCK may be a cellular target for Aurora B during mitosis.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Dulyaninova NG,Bresnick ARdoi
10.1016/j.yexcr.2004.06.015keywords:
subject
Has Abstractpub_date
2004-10-01 00:00:00pages
303-14issue
2eissn
0014-4827issn
1090-2422pii
S0014-4827(04)00358-1journal_volume
299pub_type
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journal_title:Experimental cell research
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journal_title:Experimental cell research
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