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Article: Phospho-Regulated Interaction between Kinesin-6 Klp9p and Microtubule Bundler Ase1p Promotes Spindle Elongation

TitlePhospho-Regulated Interaction between Kinesin-6 Klp9p and Microtubule Bundler Ase1p Promotes Spindle Elongation
Authors
KeywordsCELLBIO
Issue Date2009
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/devcel
Citation
Developmental Cell, 2009, v. 17 n. 2, p. 257-267 How to Cite?
AbstractThe spindle midzone-composed of antiparallel microtubules, microtubule-associated proteins (MAPs), and motors-is the structure responsible for microtubule organization and sliding during anaphase B. In general, MAPs and motors stabilize the midzone and motors produce sliding. We show that fission yeast kinesin-6 motor klp9p binds to the microtubule antiparallel bundler ase1p at the midzone at anaphase B onset. This interaction depends upon the phosphorylation states of klp9p and ase1p. The cyclin-dependent kinase cdc2p phosphorylates and its antagonist phosphatase clp1p dephosphorylates klp9p and ase1p to control the position and timing of klp9p-ase1p interaction. Failure of klp9p-ase1p binding leads to decreased spindle elongation velocity. The ase1p-mediated recruitment of klp9p to the midzone accelerates pole separation, as suggested by computer simulation. Our findings indicate that a phosphorylation switch controls the spatial-temporal interactions of motors and MAPs for proper anaphase B, and suggest a mechanism whereby a specific motor-MAP conformation enables efficient microtubule sliding. © 2009 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/136775
ISSN
2015 Impact Factor: 9.338
2015 SCImago Journal Rankings: 7.338
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Volkswagen-Stiftung
ARC
NIH
ACS
HFSP
ANR
FRM
LaLigue
Funding Information:

We thank Anabelle Decottignies, Fred Chang, Kathy Gould, Ian Hagan, Dan McCollum, and Paul Nurse for yeast strains and reagents. We thank Andrea Stout for expert technical FRAP assistance. We also thank members of Erfei Bi Lab and members of MBL Physiology 2007 for helpful discussions and advice. F.J.N. is supported by BioMS, J.W. is supported by Volkswagen-Stiftung. G.V.-C. is supported by ARC. The Tran Lab is supported by grants from NIH, ACS, HFSP, ANR, FRM, and LaLigue. C.F., I.L., G. V.-C., and P.T.T. created the reagents, performed the experiments, and analyzed the data. J.W. and F.N. performed the computer simulations. C.F.. J.W., F.N., and P.T.T. wrote the paper, and all authors made comments.

References

 

DC FieldValueLanguage
dc.contributor.authorFu, Cen_HK
dc.contributor.authorWard, JJen_HK
dc.contributor.authorLoiodice, Ien_HK
dc.contributor.authorVelveCasquillas, Gen_HK
dc.contributor.authorNedelec, FJen_HK
dc.contributor.authorTran, PTen_HK
dc.date.accessioned2011-07-29T02:11:58Z-
dc.date.available2011-07-29T02:11:58Z-
dc.date.issued2009en_HK
dc.identifier.citationDevelopmental Cell, 2009, v. 17 n. 2, p. 257-267en_HK
dc.identifier.issn1534-5807en_HK
dc.identifier.urihttp://hdl.handle.net/10722/136775-
dc.description.abstractThe spindle midzone-composed of antiparallel microtubules, microtubule-associated proteins (MAPs), and motors-is the structure responsible for microtubule organization and sliding during anaphase B. In general, MAPs and motors stabilize the midzone and motors produce sliding. We show that fission yeast kinesin-6 motor klp9p binds to the microtubule antiparallel bundler ase1p at the midzone at anaphase B onset. This interaction depends upon the phosphorylation states of klp9p and ase1p. The cyclin-dependent kinase cdc2p phosphorylates and its antagonist phosphatase clp1p dephosphorylates klp9p and ase1p to control the position and timing of klp9p-ase1p interaction. Failure of klp9p-ase1p binding leads to decreased spindle elongation velocity. The ase1p-mediated recruitment of klp9p to the midzone accelerates pole separation, as suggested by computer simulation. Our findings indicate that a phosphorylation switch controls the spatial-temporal interactions of motors and MAPs for proper anaphase B, and suggest a mechanism whereby a specific motor-MAP conformation enables efficient microtubule sliding. © 2009 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_US
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/devcelen_HK
dc.relation.ispartofDevelopmental Cellen_HK
dc.subjectCELLBIOen_HK
dc.titlePhospho-Regulated Interaction between Kinesin-6 Klp9p and Microtubule Bundler Ase1p Promotes Spindle Elongationen_HK
dc.typeArticleen_HK
dc.identifier.emailFu, C:chuanhai@hku.hken_HK
dc.identifier.authorityFu, C=rp01515en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.devcel.2009.06.012en_HK
dc.identifier.pmid19686686en_HK
dc.identifier.pmcidPMC2997714-
dc.identifier.scopuseid_2-s2.0-68349105806en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-68349105806&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume17en_HK
dc.identifier.issue2en_HK
dc.identifier.spage257en_HK
dc.identifier.epage267en_HK
dc.identifier.eissn1878-1551-
dc.identifier.isiWOS:000269138600015-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridFu, C=8583808400en_HK
dc.identifier.scopusauthoridWard, JJ=7404119660en_HK
dc.identifier.scopusauthoridLoiodice, I=8259036100en_HK
dc.identifier.scopusauthoridVelveCasquillas, G=13008971800en_HK
dc.identifier.scopusauthoridNedelec, FJ=6602974656en_HK
dc.identifier.scopusauthoridTran, PT=7102073156en_HK
dc.identifier.citeulike5469642-

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