Tags

Type your tag names separated by a space and hit enter

Cleavage furrow organization requires PIP(2)-mediated recruitment of anillin.
Curr Biol. 2012 Jan 10; 22(1):64-9.CB

Abstract

Cell division is achieved by a plasma membrane furrow that must ingress between the segregating chromosomes during anaphase [1-3]. The force that drives furrow ingression is generated by the actomyosin cytoskeleton, which is linked to the membrane by an as yet undefined molecular mechanism. A key component of the membrane furrow is anillin. Upon targeting to the furrow through its pleckstrin homology (PH) domain, anillin acts as a scaffold linking the actomyosin and septin cytoskeletons to maintain furrow stability (reviewed in [4, 5]). We report that the PH domain of anillin interacts with phosphatidylinositol phosphate lipids (PIPs), including PI(4,5)P(2), which is enriched in the furrow. Reduction of cellular PI(4,5)P(2) or mutations in the PH domain of anillin that specifically disrupt the interaction with PI(4,5)P(2), interfere with the localization of anillin to the furrow. Reduced expression of anillin disrupts symmetric furrow ingression that can be restored by targeting ectopically expressed anillin to the furrow using an alternate PI(4,5)P(2) binding module, a condition where the septin cytoskeleton is not recruited to the plasma membrane. These data demonstrate that the anillin PH domain has two functions: targeting anillin to the furrow by binding to PI(4,5)P(2) to maintain furrow organization and recruiting septins to the furrow.

Authors+Show Affiliations

Department of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22197245

Citation

Liu, Jinghe, et al. "Cleavage Furrow Organization Requires PIP(2)-mediated Recruitment of Anillin." Current Biology : CB, vol. 22, no. 1, 2012, pp. 64-9.
Liu J, Fairn GD, Ceccarelli DF, et al. Cleavage furrow organization requires PIP(2)-mediated recruitment of anillin. Curr Biol. 2012;22(1):64-9.
Liu, J., Fairn, G. D., Ceccarelli, D. F., Sicheri, F., & Wilde, A. (2012). Cleavage furrow organization requires PIP(2)-mediated recruitment of anillin. Current Biology : CB, 22(1), 64-9. https://doi.org/10.1016/j.cub.2011.11.040
Liu J, et al. Cleavage Furrow Organization Requires PIP(2)-mediated Recruitment of Anillin. Curr Biol. 2012 Jan 10;22(1):64-9. PubMed PMID: 22197245.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cleavage furrow organization requires PIP(2)-mediated recruitment of anillin. AU - Liu,Jinghe, AU - Fairn,Gregory D, AU - Ceccarelli,Derek F, AU - Sicheri,Frank, AU - Wilde,Andrew, Y1 - 2011/12/22/ PY - 2011/07/18/received PY - 2011/10/19/revised PY - 2011/11/21/accepted PY - 2011/12/27/entrez PY - 2011/12/27/pubmed PY - 2012/8/9/medline SP - 64 EP - 9 JF - Current biology : CB JO - Curr. Biol. VL - 22 IS - 1 N2 - Cell division is achieved by a plasma membrane furrow that must ingress between the segregating chromosomes during anaphase [1-3]. The force that drives furrow ingression is generated by the actomyosin cytoskeleton, which is linked to the membrane by an as yet undefined molecular mechanism. A key component of the membrane furrow is anillin. Upon targeting to the furrow through its pleckstrin homology (PH) domain, anillin acts as a scaffold linking the actomyosin and septin cytoskeletons to maintain furrow stability (reviewed in [4, 5]). We report that the PH domain of anillin interacts with phosphatidylinositol phosphate lipids (PIPs), including PI(4,5)P(2), which is enriched in the furrow. Reduction of cellular PI(4,5)P(2) or mutations in the PH domain of anillin that specifically disrupt the interaction with PI(4,5)P(2), interfere with the localization of anillin to the furrow. Reduced expression of anillin disrupts symmetric furrow ingression that can be restored by targeting ectopically expressed anillin to the furrow using an alternate PI(4,5)P(2) binding module, a condition where the septin cytoskeleton is not recruited to the plasma membrane. These data demonstrate that the anillin PH domain has two functions: targeting anillin to the furrow by binding to PI(4,5)P(2) to maintain furrow organization and recruiting septins to the furrow. SN - 1879-0445 UR - https://www.unboundmedicine.com/medline/citation/22197245/Cleavage_furrow_organization_requires_PIP_2__mediated_recruitment_of_anillin_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0960-9822(11)01322-4 DB - PRIME DP - Unbound Medicine ER -