Cargando…

Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning

Cytoplasmic dynein is a large multisubunit complex involved in retrograde transport and the positioning of various organelles. Dynein light chain (LC) subunits are conserved across species; however, the molecular contribution of LCs to dynein function remains controversial. One model suggests that L...

Descripción completa

Detalles Bibliográficos
Autores principales: Stuchell-Brereton, Melissa D., Siglin, Amanda, Li, Jun, Moore, Jeffrey K., Ahmed, Shubbir, Williams, John C., Cooper, John A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145545/
https://www.ncbi.nlm.nih.gov/pubmed/21633107
http://dx.doi.org/10.1091/mbc.E11-01-0075
_version_ 1782209091412688896
author Stuchell-Brereton, Melissa D.
Siglin, Amanda
Li, Jun
Moore, Jeffrey K.
Ahmed, Shubbir
Williams, John C.
Cooper, John A.
author_facet Stuchell-Brereton, Melissa D.
Siglin, Amanda
Li, Jun
Moore, Jeffrey K.
Ahmed, Shubbir
Williams, John C.
Cooper, John A.
author_sort Stuchell-Brereton, Melissa D.
collection PubMed
description Cytoplasmic dynein is a large multisubunit complex involved in retrograde transport and the positioning of various organelles. Dynein light chain (LC) subunits are conserved across species; however, the molecular contribution of LCs to dynein function remains controversial. One model suggests that LCs act as cargo-binding scaffolds. Alternatively, LCs are proposed to stabilize the intermediate chains (ICs) of the dynein complex. To examine the role of LCs in dynein function, we used Saccharomyces cerevisiae, in which the sole function of dynein is to position the spindle during mitosis. We report that the LC8 homologue, Dyn2, localizes with the dynein complex at microtubule ends and interacts directly with the yeast IC, Pac11. We identify two Dyn2-binding sites in Pac11 that exert differential effects on Dyn2-binding and dynein function. Mutations disrupting Dyn2 elicit a partial loss-of-dynein phenotype and impair the recruitment of the dynein activator complex, dynactin. Together these results indicate that the dynein-based function of Dyn2 is via its interaction with the dynein IC and that this interaction is important for the interaction of dynein and dynactin. In addition, these data provide the first direct evidence that LC occupancy in the dynein motor complex is important for function.
format Online
Article
Text
id pubmed-3145545
institution National Center for Biotechnology Information
language English
publishDate 2011
publisher The American Society for Cell Biology
record_format MEDLINE/PubMed
spelling pubmed-31455452011-10-16 Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning Stuchell-Brereton, Melissa D. Siglin, Amanda Li, Jun Moore, Jeffrey K. Ahmed, Shubbir Williams, John C. Cooper, John A. Mol Biol Cell Articles Cytoplasmic dynein is a large multisubunit complex involved in retrograde transport and the positioning of various organelles. Dynein light chain (LC) subunits are conserved across species; however, the molecular contribution of LCs to dynein function remains controversial. One model suggests that LCs act as cargo-binding scaffolds. Alternatively, LCs are proposed to stabilize the intermediate chains (ICs) of the dynein complex. To examine the role of LCs in dynein function, we used Saccharomyces cerevisiae, in which the sole function of dynein is to position the spindle during mitosis. We report that the LC8 homologue, Dyn2, localizes with the dynein complex at microtubule ends and interacts directly with the yeast IC, Pac11. We identify two Dyn2-binding sites in Pac11 that exert differential effects on Dyn2-binding and dynein function. Mutations disrupting Dyn2 elicit a partial loss-of-dynein phenotype and impair the recruitment of the dynein activator complex, dynactin. Together these results indicate that the dynein-based function of Dyn2 is via its interaction with the dynein IC and that this interaction is important for the interaction of dynein and dynactin. In addition, these data provide the first direct evidence that LC occupancy in the dynein motor complex is important for function. The American Society for Cell Biology 2011-08-01 /pmc/articles/PMC3145545/ /pubmed/21633107 http://dx.doi.org/10.1091/mbc.E11-01-0075 Text en © 2011 Stuchell-Brereton et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Stuchell-Brereton, Melissa D.
Siglin, Amanda
Li, Jun
Moore, Jeffrey K.
Ahmed, Shubbir
Williams, John C.
Cooper, John A.
Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
title Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
title_full Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
title_fullStr Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
title_full_unstemmed Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
title_short Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
title_sort functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145545/
https://www.ncbi.nlm.nih.gov/pubmed/21633107
http://dx.doi.org/10.1091/mbc.E11-01-0075
work_keys_str_mv AT stuchellbreretonmelissad functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning
AT siglinamanda functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning
AT lijun functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning
AT moorejeffreyk functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning
AT ahmedshubbir functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning
AT williamsjohnc functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning
AT cooperjohna functionalinteractionbetweendyneinlightchainandintermediatechainisrequiredformitoticspindlepositioning