Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport.
The microtubule-based motor dynein generates pulling forces for centrosome centration and mitotic spindle positioning in animal cells. How the essential dynein activator dynactin regulates these functions of the motor is incompletely understood. Here, we dissect the role of dynactin's microtubu...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2017-07-01
|
| Series: | PLoS Genetics |
| Online Access: | http://europepmc.org/articles/PMC5552355?pdf=render |
| _version_ | 1818969755330019328 |
|---|---|
| author | Daniel J Barbosa Joana Duro Bram Prevo Dhanya K Cheerambathur Ana X Carvalho Reto Gassmann |
| author_facet | Daniel J Barbosa Joana Duro Bram Prevo Dhanya K Cheerambathur Ana X Carvalho Reto Gassmann |
| author_sort | Daniel J Barbosa |
| collection | DOAJ |
| description | The microtubule-based motor dynein generates pulling forces for centrosome centration and mitotic spindle positioning in animal cells. How the essential dynein activator dynactin regulates these functions of the motor is incompletely understood. Here, we dissect the role of dynactin's microtubule binding activity, located in the p150 CAP-Gly domain and an adjacent basic patch, in the C. elegans zygote. Analysis of p150 mutants engineered by genome editing suggests that microtubule tip tracking of dynein-dynactin is dispensable for targeting the motor to the cell cortex and for generating robust cortical pulling forces. Instead, mutations in p150's CAP-Gly domain inhibit cytoplasmic pulling forces responsible for centration of centrosomes and attached pronuclei. The centration defects are mimicked by mutations of α-tubulin's C-terminal tyrosine, and both p150 CAP-Gly and tubulin tyrosine mutants decrease the frequency of early endosome transport from the cell periphery towards centrosomes during centration. Our results suggest that p150 GAP-Gly domain binding to tyrosinated microtubules promotes initiation of dynein-mediated organelle transport in the dividing one-cell embryo, and that this function of p150 is critical for generating cytoplasmic pulling forces for centrosome centration. |
| first_indexed | 2024-12-20T14:25:37Z |
| format | Article |
| id | doaj.art-b6cfd4153cae4f1ab432df581cdad9a9 |
| institution | Directory Open Access Journal |
| issn | 1553-7390 1553-7404 |
| language | English |
| last_indexed | 2024-12-20T14:25:37Z |
| publishDate | 2017-07-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Genetics |
| spelling | doaj.art-b6cfd4153cae4f1ab432df581cdad9a92022-12-21T19:37:48ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042017-07-01137e100694110.1371/journal.pgen.1006941Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport.Daniel J BarbosaJoana DuroBram PrevoDhanya K CheerambathurAna X CarvalhoReto GassmannThe microtubule-based motor dynein generates pulling forces for centrosome centration and mitotic spindle positioning in animal cells. How the essential dynein activator dynactin regulates these functions of the motor is incompletely understood. Here, we dissect the role of dynactin's microtubule binding activity, located in the p150 CAP-Gly domain and an adjacent basic patch, in the C. elegans zygote. Analysis of p150 mutants engineered by genome editing suggests that microtubule tip tracking of dynein-dynactin is dispensable for targeting the motor to the cell cortex and for generating robust cortical pulling forces. Instead, mutations in p150's CAP-Gly domain inhibit cytoplasmic pulling forces responsible for centration of centrosomes and attached pronuclei. The centration defects are mimicked by mutations of α-tubulin's C-terminal tyrosine, and both p150 CAP-Gly and tubulin tyrosine mutants decrease the frequency of early endosome transport from the cell periphery towards centrosomes during centration. Our results suggest that p150 GAP-Gly domain binding to tyrosinated microtubules promotes initiation of dynein-mediated organelle transport in the dividing one-cell embryo, and that this function of p150 is critical for generating cytoplasmic pulling forces for centrosome centration.http://europepmc.org/articles/PMC5552355?pdf=render |
| spellingShingle | Daniel J Barbosa Joana Duro Bram Prevo Dhanya K Cheerambathur Ana X Carvalho Reto Gassmann Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. PLoS Genetics |
| title | Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. |
| title_full | Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. |
| title_fullStr | Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. |
| title_full_unstemmed | Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. |
| title_short | Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. |
| title_sort | dynactin binding to tyrosinated microtubules promotes centrosome centration in c elegans by enhancing dynein mediated organelle transport |
| url | http://europepmc.org/articles/PMC5552355?pdf=render |
| work_keys_str_mv | AT danieljbarbosa dynactinbindingtotyrosinatedmicrotubulespromotescentrosomecentrationincelegansbyenhancingdyneinmediatedorganelletransport AT joanaduro dynactinbindingtotyrosinatedmicrotubulespromotescentrosomecentrationincelegansbyenhancingdyneinmediatedorganelletransport AT bramprevo dynactinbindingtotyrosinatedmicrotubulespromotescentrosomecentrationincelegansbyenhancingdyneinmediatedorganelletransport AT dhanyakcheerambathur dynactinbindingtotyrosinatedmicrotubulespromotescentrosomecentrationincelegansbyenhancingdyneinmediatedorganelletransport AT anaxcarvalho dynactinbindingtotyrosinatedmicrotubulespromotescentrosomecentrationincelegansbyenhancingdyneinmediatedorganelletransport AT retogassmann dynactinbindingtotyrosinatedmicrotubulespromotescentrosomecentrationincelegansbyenhancingdyneinmediatedorganelletransport |