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Interaction between Anillin and RacGAP50C connects the actomyosin contractile ring with spindle microtubules at the cell division site

D'Avino, Pier Paolo and Takeda, Tetsuya and Capalbo, Luisa and Zhang, Wei and Lilley, Kathryn S. and Laue, Ernest D. and Glover, David M. (2008) Interaction between Anillin and RacGAP50C connects the actomyosin contractile ring with spindle microtubules at the cell division site. Journal of Cell Science, 121 (8). pp. 1151-1158. ISSN 0021-9533. doi:10.1242/jcs.026716. https://resolver.caltech.edu/CaltechAUTHORS:20201002-140639400

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[img] Image (JPEG) (Fig. S1. Anillin localization is unaltered after RNAi depletion of spectrins) - Supplemental Material
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[img] Image (JPEG) (Fig. S2. RacGAP50C localization in telophase cells after Anillin RNAi) - Supplemental Material
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[img] Image (JPEG) (Fig. S3. F-actin and Anillin localization during cell division) - Supplemental Material
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[img] Image (JPEG) (Fig. S4. Latranculin-A treatment promotes microtubule stabilization) - Supplemental Material
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[img] Image (JPEG) (Fig. S5. Subcellular localization of GFP-tagged Anillin fragments) - Supplemental Material
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[img] Image (JPEG) (Fig. S6. GFP-tagged Ani_(410-1104) co-localizes with RacGAP50C in telophase) - Supplemental Material
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[img] Image (JPEG) (Fig. S7. Pnut and Sep2 do not localize to the cortex in metaphase) - Supplemental Material
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Abstract

Anillin, one of the first factors recruited to the cleavage site during cytokinesis, interacts with actin, myosin II and septins, and is essential for proper organization of the actomyosin contractile ring. We employed affinity-purification methodology coupled with mass spectrometry to identify Anillin-interacting molecules in Drosophila cells. We isolated several actin and myosin proteins, three of the five Drosophila septins and RacGAP50C (Tum), a component of the centralspindlin complex. Using drug and RNA interference (RNAi) treatments we established that F-actin is essential for Anillin cortical localization in prometaphase but not for its accumulation at the cleavage furrow after anaphase onset. Moreover, septins were not recruited to the cleavage site in cells in which Anillin was knocked down by RNAi, but localized to central-spindle microtubules, suggesting that septins travel along microtubules to interact with Anillin at the furrow. Finally, we demonstrate that RacGAP50C is necessary for Anillin accumulation at the furrow and that the two proteins colocalize in vivo and interact in vitro. Thus, in addition to its role in activating RhoA signalling, RacGAP50C also controls the proper assembly of the actomyosin ring by interacting with Anillin at the cleavage furrow.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1242/jcs.026716DOIArticle
http://jcs.biologists.org/cgi/content/full/121/8/1151/DC1PublisherSupporting Information
ORCID:
AuthorORCID
D'Avino, Pier Paolo0000-0002-4773-6950
Takeda, Tetsuya0000-0002-3183-6551
Lilley, Kathryn S.0000-0003-0594-6543
Laue, Ernest D.0000-0002-7476-4148
Glover, David M.0000-0003-0956-0103
Additional Information:© The Company of Biologists Limited 2008. Accepted January 24, 2008. Published online April 3, 2008. We are grateful to R. Dubreuil, C. Field, M. Mishima, J. Pringle and R. Saint for antibodies and reagents. We thank M. Savoian for critical reading of the manuscript. This work was supported by a CR-UK programme grant to D.M.G., and a BBSRC project grant to D.M.G., E.D.L., K.S.L. and P.P.D.
Funders:
Funding AgencyGrant Number
Cancer Research UKUNSPECIFIED
Biotechnology and Biological Sciences Research Council (BBSRC)UNSPECIFIED
Subject Keywords:Anillin, Centralspindlin, Affinity purification, Protein complex
Issue or Number:8
DOI:10.1242/jcs.026716
Record Number:CaltechAUTHORS:20201002-140639400
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20201002-140639400
Official Citation:Interaction between Anillin and RacGAP50C connects the actomyosin contractile ring with spindle microtubules at the cell division site Pier Paolo D'Avino, Tetsuya Takeda, Luisa Capalbo, Wei Zhang, Kathryn S. Lilley, Ernest D. Laue, David M. Glover Journal of Cell Science 2008 121: 1151-1158; doi: 10.1242/jcs.026716
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:105757
Collection:CaltechAUTHORS
Deposited By: George Porter
Deposited On:05 Oct 2020 14:49
Last Modified:16 Nov 2021 18:46

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