Nsl1p is essential for the establishment of bipolarity and the localization of the Dam-Duo complex.

2.50
Hdl Handle:
http://hdl.handle.net/10541/82358
Title:
Nsl1p is essential for the establishment of bipolarity and the localization of the Dam-Duo complex.
Authors:
Scharfenberger, Maren; Ortiz, Jennifer; Grau, Nicole; Janke, Carsten; Schiebel, Elmar; Lechner, Johannes
Abstract:
We identified a physical complex consisting of Mtw1p, an established kinetochore protein, with Nnf1p, Nsl1p and Dsn1p and have demonstrated that Nnf1p, Nsl1p and Dsn1p localize to the Saccharomyces cerevisiae kinetochore. When challenged prior to metaphase, the temperature-sensitive mutants nsl1-16 and nsl1-42 as well as Nsl1p-depleted cells failed to establish a bipolar spindle-kinetochore interaction and executed monopolar segregation of sister chromatids. In contrast, an nsl1-16 defect could not be evoked after the establishment of bipolarity. The observed phenotype is characteristic of that of mutants with defects in the protein kinase Ipl1p or components of the Dam-Duo kinetochore complex. However nsl1 mutants did not exhibit a defect in microtubule-kinetochore untethering as the ipl1-321 mutant does. Instead, they exhibited a severe defect in the kinetochore localization of the Dam-Duo complex suggesting this to be the cause for the failure of nsl1 cells to establish bipolarity. Moreover the analysis of Nsl1p-depleted cells indicated that Nsl1p is required for the spindle checkpoint and kinetochore integrity.
Affiliation:
Biochemie-Zentrum Heidelberg Ruprecht-Karls Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
Citation:
Nsl1p is essential for the establishment of bipolarity and the localization of the Dam-Duo complex. 2003, 22 (24):6584-97 EMBO J.
Journal:
The EMBO Journal
Issue Date:
15-Dec-2003
URI:
http://hdl.handle.net/10541/82358
DOI:
10.1093/emboj/cdg636
PubMed ID:
14657030
Type:
Article
Language:
en
ISSN:
0261-4189
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorScharfenberger, Maren-
dc.contributor.authorOrtiz, Jennifer-
dc.contributor.authorGrau, Nicole-
dc.contributor.authorJanke, Carsten-
dc.contributor.authorSchiebel, Elmar-
dc.contributor.authorLechner, Johannes-
dc.date.accessioned2009-09-23T13:32:57Z-
dc.date.available2009-09-23T13:32:57Z-
dc.date.issued2003-12-15-
dc.identifier.citationNsl1p is essential for the establishment of bipolarity and the localization of the Dam-Duo complex. 2003, 22 (24):6584-97 EMBO J.en
dc.identifier.issn0261-4189-
dc.identifier.pmid14657030-
dc.identifier.doi10.1093/emboj/cdg636-
dc.identifier.urihttp://hdl.handle.net/10541/82358-
dc.description.abstractWe identified a physical complex consisting of Mtw1p, an established kinetochore protein, with Nnf1p, Nsl1p and Dsn1p and have demonstrated that Nnf1p, Nsl1p and Dsn1p localize to the Saccharomyces cerevisiae kinetochore. When challenged prior to metaphase, the temperature-sensitive mutants nsl1-16 and nsl1-42 as well as Nsl1p-depleted cells failed to establish a bipolar spindle-kinetochore interaction and executed monopolar segregation of sister chromatids. In contrast, an nsl1-16 defect could not be evoked after the establishment of bipolarity. The observed phenotype is characteristic of that of mutants with defects in the protein kinase Ipl1p or components of the Dam-Duo kinetochore complex. However nsl1 mutants did not exhibit a defect in microtubule-kinetochore untethering as the ipl1-321 mutant does. Instead, they exhibited a severe defect in the kinetochore localization of the Dam-Duo complex suggesting this to be the cause for the failure of nsl1 cells to establish bipolarity. Moreover the analysis of Nsl1p-depleted cells indicated that Nsl1p is required for the spindle checkpoint and kinetochore integrity.en
dc.language.isoenen
dc.subject.meshCell Cycle Proteins-
dc.subject.meshCell Polarity-
dc.subject.meshCytoskeletal Proteins-
dc.subject.meshKinetochores-
dc.subject.meshMacromolecular Substances-
dc.subject.meshMicrotubule-Associated Proteins-
dc.subject.meshMitotic Spindle Apparatus-
dc.subject.meshModels, Biological-
dc.subject.meshSaccharomyces cerevisiae-
dc.subject.meshSaccharomyces cerevisiae Proteins-
dc.subject.meshSister Chromatid Exchange-
dc.subject.meshTemperature-
dc.titleNsl1p is essential for the establishment of bipolarity and the localization of the Dam-Duo complex.en
dc.typeArticleen
dc.contributor.departmentBiochemie-Zentrum Heidelberg Ruprecht-Karls Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.en
dc.identifier.journalThe EMBO Journalen
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