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Article: Mcp1p tracks microtubule plus ends to destabilize microtubules at cell tips

TitleMcp1p tracks microtubule plus ends to destabilize microtubules at cell tips
Authors
Issue Date2014
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
FEBS Letters, 2014, v. 588 n. 6, p. 859-865 How to Cite?
AbstractMicrotubule plus ends are dynamically regulated by a wide variety of proteins for performing diverse cellular functions. Here, we show that the fission yeast Schizosaccharomyces pombe uncharacterized protein mcp1p is a microtubule plus-end tracking protein which depends on the kinesin-8 klp6p for transporting along microtubules towards microtubule plus ends. In the absence of mcp1p, microtubule catastrophe and rescue frequencies decrease, leading to an increased dwell time of microtubule plus ends at cell tips. Thus, these findings suggest that mcp1p may synergize with klp6p at microtubule plus-ends to destabilize microtubules.
Persistent Identifierhttp://hdl.handle.net/10722/194951
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZheng, Fen_US
dc.contributor.authorLi, Ten_US
dc.contributor.authorCheung, MCHen_US
dc.contributor.authorSyrovatkina, Ven_US
dc.contributor.authorFu, Cen_US
dc.date.accessioned2014-02-21T06:39:23Z-
dc.date.available2014-02-21T06:39:23Z-
dc.date.issued2014-
dc.identifier.citationFEBS Letters, 2014, v. 588 n. 6, p. 859-865en_US
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/10722/194951-
dc.description.abstractMicrotubule plus ends are dynamically regulated by a wide variety of proteins for performing diverse cellular functions. Here, we show that the fission yeast Schizosaccharomyces pombe uncharacterized protein mcp1p is a microtubule plus-end tracking protein which depends on the kinesin-8 klp6p for transporting along microtubules towards microtubule plus ends. In the absence of mcp1p, microtubule catastrophe and rescue frequencies decrease, leading to an increased dwell time of microtubule plus ends at cell tips. Thus, these findings suggest that mcp1p may synergize with klp6p at microtubule plus-ends to destabilize microtubules.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet-
dc.relation.ispartofFEBS Lettersen_US
dc.titleMcp1p tracks microtubule plus ends to destabilize microtubules at cell tipsen_US
dc.typeArticleen_US
dc.identifier.emailCheung, MCH: mcheung9@hku.hken_US
dc.identifier.emailFu, C: chuanhai@hku.hken_US
dc.identifier.authorityCheung, MCH=rp00245en_US
dc.identifier.authorityFu, C=rp01515en_US
dc.identifier.doi10.1016/j.febslet.2014.01.055en_US
dc.identifier.pmid24530531-
dc.identifier.hkuros228055en_US
dc.identifier.hkuros240729-
dc.identifier.volume588-
dc.identifier.issue6-
dc.identifier.spage859-
dc.identifier.epage865-
dc.identifier.isiWOS:000333088800003-
dc.publisher.placeNetherlands-

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