Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1083/jcb.200812167
- Scopus: eid_2-s2.0-66349120139
- PMID: 19468067
- WOS: WOS:000266912100011
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Mitotic control of kinetochore-associated dynein and spindle orientation by human Spindly
Title | Mitotic control of kinetochore-associated dynein and spindle orientation by human Spindly |
---|---|
Authors | |
Issue Date | 2009 |
Citation | Journal of Cell Biology, 2009, v. 185, n. 5, p. 859-874 How to Cite? |
Abstract | Mitotic spindle formation and chromosome segregation depend critically on kinetochore-microtubule (KT-MT) interactions. A new protein, termed Spindly in Drosophila and SPDL-1 in C. elegans, was recently shown to regulate KT localization of dynein, but depletion phenotypes revealed striking differences, suggesting evolutionarily diverse roles of mitotic dynein. By characterizing the function of Spindly in human cells, we identify specific functions for KT dynein. We show that localization of human Spindly (hSpindly) to KTs is controlled by the Rod/Zw10/Zwilch (RZZ) complex and Aurora B. hSpindly depletion results in reduced inter-KT tension, unstable KT fibers, an extensive prometaphase delay, and severe chromosome misalignment. Moreover, depletion of hSpindly induces a striking spindle rotation, which can be rescued by co-depletion of dynein. However, in contrast to Drosophila, hSpindly depletion does not abolish the removal of MAD2 and ZW10 from KTs. Collectively, our data reveal hSpindly-mediated dynein functions and highlight a critical role of KT dynein in spindle orientation. © 2009 Chan et al. |
Persistent Identifier | http://hdl.handle.net/10722/268635 |
ISSN | 2023 Impact Factor: 7.4 2023 SCImago Journal Rankings: 3.717 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Ying, Wai Chan | - |
dc.contributor.author | Fava, Luca L. | - |
dc.contributor.author | Uldschmid, Andreas | - |
dc.contributor.author | Schmitz, Michael H.A. | - |
dc.contributor.author | Gerlich, Daniel W. | - |
dc.contributor.author | Nigg, Erich A. | - |
dc.contributor.author | Santamaria, Anna | - |
dc.date.accessioned | 2019-03-25T08:00:16Z | - |
dc.date.available | 2019-03-25T08:00:16Z | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Journal of Cell Biology, 2009, v. 185, n. 5, p. 859-874 | - |
dc.identifier.issn | 0021-9525 | - |
dc.identifier.uri | http://hdl.handle.net/10722/268635 | - |
dc.description.abstract | Mitotic spindle formation and chromosome segregation depend critically on kinetochore-microtubule (KT-MT) interactions. A new protein, termed Spindly in Drosophila and SPDL-1 in C. elegans, was recently shown to regulate KT localization of dynein, but depletion phenotypes revealed striking differences, suggesting evolutionarily diverse roles of mitotic dynein. By characterizing the function of Spindly in human cells, we identify specific functions for KT dynein. We show that localization of human Spindly (hSpindly) to KTs is controlled by the Rod/Zw10/Zwilch (RZZ) complex and Aurora B. hSpindly depletion results in reduced inter-KT tension, unstable KT fibers, an extensive prometaphase delay, and severe chromosome misalignment. Moreover, depletion of hSpindly induces a striking spindle rotation, which can be rescued by co-depletion of dynein. However, in contrast to Drosophila, hSpindly depletion does not abolish the removal of MAD2 and ZW10 from KTs. Collectively, our data reveal hSpindly-mediated dynein functions and highlight a critical role of KT dynein in spindle orientation. © 2009 Chan et al. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of Cell Biology | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Mitotic control of kinetochore-associated dynein and spindle orientation by human Spindly | - |
dc.type | Article | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1083/jcb.200812167 | - |
dc.identifier.pmid | 19468067 | - |
dc.identifier.pmcid | PMC2711594 | - |
dc.identifier.scopus | eid_2-s2.0-66349120139 | - |
dc.identifier.volume | 185 | - |
dc.identifier.issue | 5 | - |
dc.identifier.spage | 859 | - |
dc.identifier.epage | 874 | - |
dc.identifier.eissn | 0021-9525 | - |
dc.identifier.isi | WOS:000266912100011 | - |
dc.identifier.f1000 | 1159869 | - |
dc.identifier.issnl | 0021-9525 | - |