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A mutation in γ-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein Pkl1p
dc.contributor.author | Paluh, Janet L. | |
dc.contributor.author | Nogales, Eva | |
dc.contributor.author | Oakley, Berl R. | |
dc.contributor.author | McDonald, Kent | |
dc.contributor.author | Pidoux, Alison | |
dc.contributor.author | Cande, W. Z. | |
dc.date.accessioned | 2015-04-21T21:03:31Z | |
dc.date.available | 2015-04-21T21:03:31Z | |
dc.date.issued | 2000-04-01 | |
dc.identifier.citation | Paluh, J., Nogales, E., Oakley, B., McDonald, K., Pidoux, A., & Cande, W. (2000). A mutation in γ-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein Pkl1p. Moleculary Biology of the Cell, 11(4), 1225-1239. http://www.dx.doi.org/10.1091/mbc.11.4.1225 | en_US |
dc.identifier.issn | 1059-1524 | |
dc.identifier.uri | http://hdl.handle.net/1808/17459 | |
dc.description | This is the publisher's version, also available electronically from "http://www.molbiolcell.org". | en_US |
dc.description.abstract | Mitotic segregation of chromosomes requires spindle pole functions for microtubule nucleation, minus end organization, and regulation of dynamics. γ-Tubulin is essential for nucleation, and we now extend its role to these latter processes. We have characterized a mutation in γ-tubulin that results in cold-sensitive mitotic arrest with an elongated bipolar spindle but impaired anaphase A. At 30°C cytoplasmic microtubule arrays are abnormal and bundle into single larger arrays. Three-dimensional time-lapse video microscopy reveals that microtubule dynamics are altered. Localization of the mutant γ-tubulin is like the wild-type protein. Prediction of γ-tubulin structure indicates that non-α/β-tubulin protein–protein interactions could be affected. The kinesin-like protein (klp)Pkl1p localizes to the spindle poles and spindle and is essential for viability of the γ-tubulin mutant and in multicopy for normal cell morphology at 30°C. Localization and function of Pkl1p in the mutant appear unaltered, consistent with a redundant function for this protein in wild type. Our data indicate a broader role for γ-tubulin at spindle poles in regulating aspects of microtubule dynamics and organization. We propose that Pkl1p rescues an impaired function of γ-tubulin that involves non-tubulin protein–protein interactions, presumably with a second motor, MAP, or MTOC component. | en_US |
dc.publisher | American Society for Cell Biology | en_US |
dc.title | A mutation in γ-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein Pkl1p | en_US |
dc.type | Article | |
kusw.kuauthor | Oakley, Berl R. | |
kusw.kudepartment | Molecular Biosciences | en_US |
dc.identifier.doi | 10.1091/mbc.11.4.1225 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item does not meet KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |