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Article: Mmb1p binds mitochondria to dynamic microtubules

TitleMmb1p binds mitochondria to dynamic microtubules
Authors
Issue Date2011
PublisherCell Press. The Journal's web site is located at http://www.current-biology.com/
Citation
Current Biology, 2011, v. 21 n. 17, p. 1431-1439 How to Cite?
AbstractBackground: Mitochondria form a dynamic tubular network within the cell. Proper mitochondria movement and distribution are critical for their localized function in cell metabolism, growth, and survival. In mammalian cells, mechanisms of mitochondria positioning appear dependent on the microtubule cytoskeleton, with kinesin or dynein motors carrying mitochondria as cargos and distributing them throughout the microtubule network. Interestingly, the timescale of microtubule dynamics occurs in seconds, and the timescale of mitochondria distribution occurs in minutes. How does the cell couple these two time constants? Results: Fission yeast also relies on microtubules for mitochondria distribution. We report here a new microtubule-dependent but motor-independent mechanism for proper mitochondria positioning in fission yeast. We identify the protein mmb1p, which binds to mitochondria and microtubules. mmb1p attaches the tubular mitochondria to the microtubule lattice at multiple discrete interaction sites. mmb1 deletion causes mitochondria to aggregate, with the long-term consequence of defective mitochondria distribution and cell death. mmb1p decreases microtubule dynamicity. Conclusions: mmb1p is a new microtubule-mitochondria binding protein. We propose that mmb1p acts to couple long-term mitochondria distribution to short-term microtubule dynamics by attenuating microtubule dynamics, thus enhancing the mitochondria-microtubule interaction time. © 2011 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/147638
ISSN
2015 Impact Factor: 8.983
2015 SCImago Journal Rankings: 4.729
ISI Accession Number ID
Funding AgencyGrant Number
FCT through Complexite du Vivant
UPMC
NIH
ACS
ANR
FRM
LaLigue
HFSP
Funding Information:

C.F., D.J., J.C., and G.V.-C. created tools and reagents and performed experiments. C.F. and P.T.T. analyzed the data and wrote the paper. We thank F. Chang (Columbia University), F. Chiron (UCSD), A. Paoletti (Institute Curie), M. Sato (Tokyo University), T. Toda (CRUK), and M.P. Yaffe (UCSD) for kindly providing reagents. We thank L. Pon (Columbia University) and A. Paoletti (Institut Curie) for helpful discussions. We thank members of the labs of E. Bi (Penn) and P.T.T. (Penn) for helpful discussions. J.C. is supported by a PhD fellowship from the FCT through Complexite du Vivant, UPMC. This work is supported by grants from NIH, ACS, ANR, FRM, LaLigue, and HFSP.

References

 

DC FieldValueLanguage
dc.contributor.authorFu, Cen_US
dc.contributor.authorJain, Den_US
dc.contributor.authorCosta, Jen_US
dc.contributor.authorVelveCasquillas, Gen_US
dc.contributor.authorTran, PTen_US
dc.date.accessioned2012-05-29T06:05:08Z-
dc.date.available2012-05-29T06:05:08Z-
dc.date.issued2011en_US
dc.identifier.citationCurrent Biology, 2011, v. 21 n. 17, p. 1431-1439en_US
dc.identifier.issn0960-9822en_US
dc.identifier.urihttp://hdl.handle.net/10722/147638-
dc.description.abstractBackground: Mitochondria form a dynamic tubular network within the cell. Proper mitochondria movement and distribution are critical for their localized function in cell metabolism, growth, and survival. In mammalian cells, mechanisms of mitochondria positioning appear dependent on the microtubule cytoskeleton, with kinesin or dynein motors carrying mitochondria as cargos and distributing them throughout the microtubule network. Interestingly, the timescale of microtubule dynamics occurs in seconds, and the timescale of mitochondria distribution occurs in minutes. How does the cell couple these two time constants? Results: Fission yeast also relies on microtubules for mitochondria distribution. We report here a new microtubule-dependent but motor-independent mechanism for proper mitochondria positioning in fission yeast. We identify the protein mmb1p, which binds to mitochondria and microtubules. mmb1p attaches the tubular mitochondria to the microtubule lattice at multiple discrete interaction sites. mmb1 deletion causes mitochondria to aggregate, with the long-term consequence of defective mitochondria distribution and cell death. mmb1p decreases microtubule dynamicity. Conclusions: mmb1p is a new microtubule-mitochondria binding protein. We propose that mmb1p acts to couple long-term mitochondria distribution to short-term microtubule dynamics by attenuating microtubule dynamics, thus enhancing the mitochondria-microtubule interaction time. © 2011 Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherCell Press. The Journal's web site is located at http://www.current-biology.com/en_US
dc.relation.ispartofCurrent Biologyen_US
dc.subject.meshCell Cycleen_US
dc.subject.meshCytoskeleton - Metabolism - Ultrastructureen_US
dc.subject.meshMicroscopy, Electron, Transmissionen_US
dc.subject.meshMicroscopy, Fluorescenceen_US
dc.subject.meshMicrotubule-Associated Proteins - Metabolismen_US
dc.subject.meshMicrotubules - Metabolism - Ultrastructureen_US
dc.subject.meshMitochondria - Metabolism - Ultrastructureen_US
dc.subject.meshSchizosaccharomyces - Cytology - Metabolism - Ultrastructureen_US
dc.subject.meshSchizosaccharomyces Pombe Proteins - Metabolismen_US
dc.titleMmb1p binds mitochondria to dynamic microtubulesen_US
dc.typeArticleen_US
dc.identifier.emailFu, C:chuanhai@hku.hken_US
dc.identifier.authorityFu, C=rp01515en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.cub.2011.07.013en_US
dc.identifier.pmid21856157-
dc.identifier.scopuseid_2-s2.0-80052814012en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-80052814012&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume21en_US
dc.identifier.issue17en_US
dc.identifier.spage1431en_US
dc.identifier.epage1439en_US
dc.identifier.eissn1879-0445-
dc.identifier.isiWOS:000295064900016-
dc.publisher.placeUnited Statesen_US
dc.identifier.f100013327991-
dc.identifier.scopusauthoridFu, C=8583808400en_US
dc.identifier.scopusauthoridJain, D=52463843200en_US
dc.identifier.scopusauthoridCosta, J=7402461239en_US
dc.identifier.scopusauthoridVelveCasquillas, G=13008971800en_US
dc.identifier.scopusauthoridTran, PT=7102073156en_US
dc.identifier.citeulike9712758-

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