XKCM1 acts on a single protofilament and requires the C terminus of tubulin
- PMID: 11866534
- DOI: 10.1006/jmbi.2001.5360
XKCM1 acts on a single protofilament and requires the C terminus of tubulin
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 state of tubulin, are stable only under conditions that inhibit XKCM1 depolymerizing activity, but can be stabilized by XKCM1 bound to AMPPNP. Tubulin polymers made of subtilisin-treated tubulin (lacking the tubulin C-terminal tail) are resistant to XKCM1-induced depolymerization, suggesting that the interaction of the acidic tail of tubulin with basic residues in XKCM1 unique to Kin I proteins is required for depolymerization.
Copyright 2002 Elsevier Science Ltd.
Similar articles
-
XMAP215 is a long thin molecule that does not increase microtubule stiffness.J Cell Sci. 2001 Aug;114(Pt 16):3025-33. doi: 10.1242/jcs.114.16.3025. J Cell Sci. 2001. PMID: 11686305
-
A new look at the microtubule binding patterns of dimeric kinesins.J Mol Biol. 2000 Apr 14;297(5):1087-103. doi: 10.1006/jmbi.2000.3627. J Mol Biol. 2000. PMID: 10764575
-
Reconstitution of physiological microtubule dynamics using purified components.Science. 2001 Nov 9;294(5545):1340-3. doi: 10.1126/science.1064629. Science. 2001. PMID: 11701928
-
Tubulin rings: which way do they curve?Curr Opin Struct Biol. 2003 Apr;13(2):256-61. doi: 10.1016/s0959-440x(03)00029-0. Curr Opin Struct Biol. 2003. PMID: 12727521 Review.
-
Microtubule dynamics and tubulin interacting proteins.Curr Opin Cell Biol. 2000 Feb;12(1):52-6. doi: 10.1016/s0955-0674(99)00056-3. Curr Opin Cell Biol. 2000. PMID: 10679354 Review.
Cited by
-
K-loop insertion restores microtubule depolymerizing activity of a "neckless" MCAK mutant.J Cell Biol. 2002 Nov 25;159(4):557-62. doi: 10.1083/jcb.200205089. J Cell Biol. 2002. PMID: 12446739 Free PMC article.
-
The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch.Elife. 2015 Apr 27;4:e06421. doi: 10.7554/eLife.06421. Elife. 2015. PMID: 25915621 Free PMC article.
-
Mitotic centromere-associated kinesin (MCAK): a potential cancer drug target.Oncotarget. 2011 Dec;2(12):935-47. doi: 10.18632/oncotarget.416. Oncotarget. 2011. PMID: 22249213 Free PMC article. Review.
-
The molecular basis for kinesin functional specificity during mitosis.Cytoskeleton (Hoboken). 2013 Sep;70(9):476-93. doi: 10.1002/cm.21135. Epub 2013 Oct 8. Cytoskeleton (Hoboken). 2013. PMID: 24039047 Free PMC article. Review.
-
Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate.Nat Commun. 2018 Jul 6;9(1):2628. doi: 10.1038/s41467-018-05025-7. Nat Commun. 2018. PMID: 29980677 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
