publication . Article . 2002

XKCM1 acts on a single protofilament and requires the C terminus of tubulin

Hanspeter Niederstrasser; Hani Salehi-Had; Eugene C. Gan; Claire E. Walczak; Eva Nogales;
Open Access
  • Published: 06 Oct 2002 Journal: Journal of Molecular Biology, volume 316, pages 817-828 (issn: 0022-2836, Copyright policy)
  • Publisher: Elsevier BV
Abstract
The stability of microtubules during the cell-cycle is regulated by a number of cellular factors, some of which stabilize microtubules and others that promote breakdown. XKCM1 is a kinesin-like protein that induces microtubule depolymerization and is required for mitotic spindle assembly. We have examined the binding and depolymerization effects of XKCM1 on different tubulin polymers in order to learn about its mechanism of action. Zinc-induced tubulin polymers, characterized by an anti-parallel protofilament arrangement, are depolymerized by XKCM1, indicating that this enzyme acts on a single protofilament. GDP-tubulin rings, which correspond to the low-energy ...
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Subjects
Medical Subject Headings: macromolecular substances
free text keywords: Molecular Biology, Guanosine diphosphate, chemistry.chemical_compound, chemistry, Depolymerization, Biology, Tubulin, biology.protein, Mechanism of action, medicine.symptom, medicine, Peptide sequence, C-terminus, Cell biology, Microtubule, Kinesin
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