Linked Life Data

1868838

Source:http://linkedlifedata.com/resource/pubmed/id/1868838

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pubmed-article:1868838pubmed:abstractTextMutation of nimA reversibly arrests cells in late G2 and nimA overexpression promotes premature mitosis. Here we demonstrate that the product of nimA (designated NIMA) has protein kinase activity that can phosphorylate beta-casein but not histone proteins. NIMA kinase activity is cell cycle regulated being 20-fold higher at mitosis when compared to S-phase arrested cells. NIMA activation is normally required in G2 to initiate chromosome condensation, to nucleate spindle pole body microtubules, and to allow an MPM-2 specific mitotic phosphorylation. All three of these mitotic events can occur in the absence of activated NIMA when the bimE gene is mutated (bimE7). However, the bimE7 mutation cannot completely bypass the requirement for nimA during mitosis as entry into mitosis in the absence of NIMA activation results in major mitotic defects that affect both the organization of the nuclear envelope and mitotic spindle. Thus, although nimA plays an essential but limited role during mitosis, mutation of nimA arrests all of mitosis. We therefore propose that mutation of nimA prevents mitotic initiation due to a checkpoint arrest that is negatively mediated by bimE. The checkpoint ensures that mitosis is not initiated until NIMA is mitotically activated.lld:pubmed
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pubmed-article:1868838pubmed:articleTitleActivation of the nimA protein kinase plays a unique role during mitosis that cannot be bypassed by absence of the bimE checkpoint.lld:pubmed
pubmed-article:1868838pubmed:affiliationDepartment of Cell Biology, Baylor College of Medicine, Houston, TX 77030.lld:pubmed
pubmed-article:1868838pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1868838pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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