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ECB-ART-31643
J Cell Biol 1990 Nov 01;1115 Pt 1:1763-73. doi: 10.1083/jcb.111.5.1763.
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Multifunctional Ca2+/calmodulin-dependent protein kinase is necessary for nuclear envelope breakdown.

Baitinger C , Alderton J , Poenie M , Schulman H , Steinhardt RA .


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The role of multifunctional Ca2+/calmodulin-dependent protein kinase (CaM kinase) in nuclear envelope breakdown (NEB) was investigated in sea urchin eggs. The eggs contain a 56-kD polypeptide which appears to be a homologue of neuronal CaM kinase. For example, it undergoes Ca2+/calmodulin-dependent autophosphorylation that converts it to a Ca2(+)-independent species, a hallmark of multifunctional CaM kinase. It is homologous to the alpha subunit of rat brain CaM kinase. Autophosphorylation and substrate phosphorylation by the sea urchin egg kinase are inhibited in vitro by CaMK(273-302), a synthetic peptide corresponding to the autoinhibitory domain of the neuronal CaM kinase. This peptide inhibited NEB when microinjected into sea urchin eggs. Only one mAb to the neuronal enzyme immunoprecipitated the 56-kD polypeptide. Only this antibody blocked or significantly delayed NEB when microinjected into sea urchin eggs. These results suggest that sea urchin eggs contain multifunctional CaM kinase, and that this enzyme is involved in the control of NEB during mitotic division.

???displayArticle.pubmedLink??? 2229172
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???displayArticle.link??? J Cell Biol
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Genes referenced: LOC100887844 LOC586799

References [+] :
Bennett, Deduced primary structure of the beta subunit of brain type II Ca2+/calmodulin-dependent protein kinase determined by molecular cloning. 1987, Pubmed