An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.

Cytokinesis occurs due to the RhoA-dependent ingression of an actomyosin ring. During anaphase, the Rho GEF (guanine nucleotide exchange factor) Ect2 is recruited to the central spindle via its interaction with MgcRacGAP/Cyk-4, and activates RhoA in the central plane of the cell. Ect2 also localizes...

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Autores principales:	Paul Frenette, Eric Haines, Michael Loloyan, Mena Kinal, Paknoosh Pakarian, Alisa Piekny
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7cb85ce4c9d144cf98ba1930939fa0b0
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spelling	oai:doaj.org-article:7cb85ce4c9d144cf98ba1930939fa0b02021-11-18T07:22:14ZAn anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.1932-620310.1371/journal.pone.0034888https://doaj.org/article/7cb85ce4c9d144cf98ba1930939fa0b02012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22514687/?tool=EBIhttps://doaj.org/toc/1932-6203Cytokinesis occurs due to the RhoA-dependent ingression of an actomyosin ring. During anaphase, the Rho GEF (guanine nucleotide exchange factor) Ect2 is recruited to the central spindle via its interaction with MgcRacGAP/Cyk-4, and activates RhoA in the central plane of the cell. Ect2 also localizes to the cortex, where it has access to RhoA. The N-terminus of Ect2 binds to Cyk-4, and the C-terminus contains conserved DH (Dbl homologous) and PH (Pleckstrin Homology) domains with GEF activity. The PH domain is required for Ect2's cortical localization, but its molecular function is not known. In cultured human cells, we found that the PH domain interacts with anillin, a contractile ring protein that scaffolds actin and myosin and interacts with RhoA. The anillin-Ect2 interaction may require Ect2's association with lipids, since a novel mutation in the PH domain, which disrupts phospholipid association, weakens their interaction. An anillin-RacGAP50C (homologue of Cyk-4) complex was previously described in Drosophila, which may crosslink the central spindle to the cortex to stabilize the position of the contractile ring. Our data supports an analogous function for the anillin-Ect2 complex in human cells and one hypothesis is that this complex has functionally replaced the Drosophila anillin-RacGAP50C complex. Complexes between central spindle proteins and cortical proteins could regulate the position of the contractile ring by stabilizing microtubule-cortical interactions at the division plane to ensure the generation of active RhoA in a discrete zone.Paul FrenetteEric HainesMichael LoloyanMena KinalPaknoosh PakarianAlisa PieknyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e34888 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Paul Frenette Eric Haines Michael Loloyan Mena Kinal Paknoosh Pakarian Alisa Piekny An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
description	Cytokinesis occurs due to the RhoA-dependent ingression of an actomyosin ring. During anaphase, the Rho GEF (guanine nucleotide exchange factor) Ect2 is recruited to the central spindle via its interaction with MgcRacGAP/Cyk-4, and activates RhoA in the central plane of the cell. Ect2 also localizes to the cortex, where it has access to RhoA. The N-terminus of Ect2 binds to Cyk-4, and the C-terminus contains conserved DH (Dbl homologous) and PH (Pleckstrin Homology) domains with GEF activity. The PH domain is required for Ect2's cortical localization, but its molecular function is not known. In cultured human cells, we found that the PH domain interacts with anillin, a contractile ring protein that scaffolds actin and myosin and interacts with RhoA. The anillin-Ect2 interaction may require Ect2's association with lipids, since a novel mutation in the PH domain, which disrupts phospholipid association, weakens their interaction. An anillin-RacGAP50C (homologue of Cyk-4) complex was previously described in Drosophila, which may crosslink the central spindle to the cortex to stabilize the position of the contractile ring. Our data supports an analogous function for the anillin-Ect2 complex in human cells and one hypothesis is that this complex has functionally replaced the Drosophila anillin-RacGAP50C complex. Complexes between central spindle proteins and cortical proteins could regulate the position of the contractile ring by stabilizing microtubule-cortical interactions at the division plane to ensure the generation of active RhoA in a discrete zone.
format	article
author	Paul Frenette Eric Haines Michael Loloyan Mena Kinal Paknoosh Pakarian Alisa Piekny
author_facet	Paul Frenette Eric Haines Michael Loloyan Mena Kinal Paknoosh Pakarian Alisa Piekny
author_sort	Paul Frenette
title	An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
title_short	An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
title_full	An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
title_fullStr	An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
title_full_unstemmed	An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
title_sort	anillin-ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/7cb85ce4c9d144cf98ba1930939fa0b0
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An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis.

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