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Importin-binding mediates the intramolecular regulation of anillin during cytokinesis.

Author(s): Beaudet D, Pham N, Skaik N, Piekny A

Mol Biol Cell. 2020 Apr 02;:mbcE20010006 Authors: Beaudet D, Pham N, Skaik N, Piekny A

Article GUID: 32238082
Hof1 plays a checkpoint related role in MMS induced DNA damage response in Candida albicans.

Author(s): Feng J, Islam A, Bean B, Feng J, Sparapani S, Shrivastava M, Goyal A, Omran RP, Mallick J, Whiteway M

Mol Biol Cell. 2020 Jan 15;:mbcE19060316 Authors: Feng J, Islam A, Bean B, Feng J, Sparapani S, Shrivastava M, Goyal A, Omran RP, Mallick J, Whiteway M

Article GUID: 31940254
Characterization of a novel separase-interacting protein and candidate new securin, Eip1p, in the fungal pathogen Candida albicans

Author(s): Sparapani S; Bachewich C;

Proper chromosome segregation is crucial for maintaining genomic stability and dependent on separase, a conserved and essential cohesin protease. Securins are key regulators of separases, but remain elusive in many organisms due to sequence divergence. Here...

Article GUID: 31411946
Active Ran regulates anillin function during cytokinesis.

Author(s): Beaudet D, Akhshi T, Phillipp J, Law C, Piekny A

Mol Biol Cell. 2017 Nov 15;28(24):3517-3531 Authors: Beaudet D, Akhshi T, Phillipp J, Law C, Piekny A

Article GUID: 28931593
The Na+(K+)/H+ exchanger Nhx1 controls multivesicular body-vacuolar lysosome fusion.

Author(s): Karim MA, Brett CL

Mol Biol Cell. 2018 02 01;29(3):317-325 Authors: Karim MA, Brett CL

Article GUID: 29212874
The adaptor protein Ste50 directly modulates yeast MAPK signaling specificity through differential connections of its RA domain.

Author(s): Sharmeen N, Sulea T, Whiteway M, Wu C

Mol Biol Cell. 2019 03 15;30(6):794-807 Authors: Sharmeen N, Sulea T, Whiteway M, Wu C

Article GUID: 30650049
Title:Active Ran regulates anillin function during cytokinesis.
Authors:Beaudet D,  Akhshi T,  Phillipp J,  Law C,  Piekny A
Link:https://www.ncbi.nlm.nih.gov/pubmed/28931593?dopt=Abstract
DOI:10.1091/mbc.E17-04-0253
Category:Mol Biol Cell
PMID:28931593
Dept Affiliation: BIOLOGY
1 Department of Biology, Concordia University, Montreal, QC H4B 1R6, Canada.
2 Program in Cell Biology, the Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.
3 Department of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
4 Centre for Microscopy and Cellular Imaging, Concordia University, Montreal, QC H4B 1R6, Canada.
5 Program in Cell Biology, the Hospital for Sick Children, Toronto, ON M5G 0A4, Canada alisa.piekny@concordia.ca.

Description:

Active Ran regulates anillin function during cytokinesis.

Mol Biol Cell. 2017 Nov 15;28(24):3517-3531

Authors: Beaudet D, Akhshi T, Phillipp J, Law C, Piekny A

Abstract

Cytokinesis cleaves a cell into two daughters at the end of mitosis, and must be spatially coordinated with chromosome segregation to prevent aneuploidy. The dogma is that the mitotic spindle governs the assembly and constriction of an actomyosin ring. Here, we reveal a function for active Ran in spatially restricting the ring. Our model is that during anaphase, "free" importins, whose gradient inversely correlates with active Ran and chromatin position, function as a molecular ruler for the recruitment and localization of anillin, a contractile protein and a crucial regulator of cytokinesis. We found that decreasing Ran-GTP levels or tethering active Ran to the equatorial membrane affects anillin's localization and causes cytokinesis phenotypes. Anillin contains a conserved nuclear localization signal (NLS) at its C-terminus that binds to importin-ß and is required for cortical polarity and cytokinesis. Mutating the NLS decreases anillin's cortical affinity, causing it to be more dominantly regulated by microtubules. Anillin contains a RhoA-GTP binding domain, which autoinhibits the NLS and the neighboring microtubule-binding domain, and RhoA-GTP binding may relieve this inhibition during mitosis. Retention of the C-terminal NLS in anillin homologues suggests that this is a conserved mechanism for controlling anillin function.

PMID: 28931593 [PubMed - indexed for MEDLINE]