Format

Send to

Choose Destination
Curr Biol. 2014 Jun 2;24(11):1263-70. doi: 10.1016/j.cub.2014.04.021. Epub 2014 May 15.

Anillin regulates cell-cell junction integrity by organizing junctional accumulation of Rho-GTP and actomyosin.

Author information

1
The Cellular and Molecular Biology Program, University of Michigan, Ann Arbor, MI 48109, USA.
2
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
3
Biomedical Imaging Group, École Polytechnique Fédérale de Lausanne, Lausanne 1015, Switzerland.
4
Centre for Systems Biology, School of Biological Sciences, The University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, Scotland, UK.
5
The Cellular and Molecular Biology Program, University of Michigan, Ann Arbor, MI 48109, USA; Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: annlm@umich.edu.

Abstract

Anillin is a scaffolding protein that organizes and stabilizes actomyosin contractile rings and was previously thought to function primarily in cytokinesis [1-10]. Using Xenopus laevis embryos as a model system to examine Anillin's role in the intact vertebrate epithelium, we find that a population of Anillin surprisingly localizes to epithelial cell-cell junctions throughout the cell cycle, whereas it was previously thought to be nuclear during interphase [5, 11]. Furthermore, we show that Anillin plays a critical role in regulating cell-cell junction integrity. Both tight junctions and adherens junctions are disrupted when Anillin is knocked down, leading to altered cell shape and increased intercellular spaces. Anillin interacts with Rho, F-actin, and myosin II [3, 8, 9], all of which regulate cell-cell junction structure and function. When Anillin is knocked down, active Rho (Rho-guanosine triphosphate [GTP]), F-actin, and myosin II are misregulated at junctions. Indeed, increased dynamic "flares" of Rho-GTP are observed at cell-cell junctions, whereas overall junctional F-actin and myosin II accumulation is reduced when Anillin is depleted. We propose that Anillin is required for proper Rho-GTP distribution at cell-cell junctions and for maintenance of a robust apical actomyosin belt, which is required for cell-cell junction integrity. These results reveal a novel role for Anillin in regulating epithelial cell-cell junctions.

PMID:
24835458
PMCID:
PMC4043929
DOI:
10.1016/j.cub.2014.04.021
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center