Kinesin-related proteins at mitotic spindle poles: function and regulation
Article Abstract:
The homologs of the bimC family of kinesin-related proteins are necessary for mitotic spindle assembly. The homologs of the bimC family of proteins are present in diverse organisms such as Drosophila, yeast, Xenopus and humans indicating that they are conserved during evolution. The bimC proteins cross-link microtubules and push spindle poles apart. Phosphorylation of bimC homologs is essential for mitotic spindle localization. Phosphorylation appears to regulate bimC tetramerization or its interaction with microtubules.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
Article Abstract:
A small, heat stable protein that physically interacts with tubulin dimers and enhances the destruction rate of microtubules was discovered. The protein was identified as oncoprotein 18 (Op18)/stathmin, a conserved phosphoprotein that is abundant in leukemia cells. Findings indicated that Op18/stathmin controls microtubules and prefers to interact with unpolymerized subunits. The protein can be used for enhancing microtubule destruction rate in mitosis and for controlling microtubule dynamics from external stimuli.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Kin I kinesins are microtubule-destabilizing enzymes
Article Abstract:
A study was conducted to show that two members of the internal catalytic domain kinesin subfamily catalytically destabilize microtubules using a unique mechanism. The members, XKCM1 and XKIF2, inffluence microtubuele stability by targeting directly to microtubule ends to induce a destablizing conformational change. The physical disruption of end structure is supported by a negative stain analysis.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1999
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