Arv1 promotes cell division by recruiting IQGAP1 and myosin to the cleavage furrow

Abstract

Cell division is strictly regulated by a diversity of proteins and lipids to ensure proper duplication and segregation of genetic material and organelles. Here we report a novel role of the putative lipid transporter ACAT-related protein required for viability 1 (Arv1) during telophase. We observed that the subcellular localization of Arv1 changes according to cell cycle progression and that Arv1 is recruited to the cleavage furrow in early telophase by epithelial protein lost in neoplasm (EPLIN). At the cleavage furrow Arv1 recruits myosin heavy chain 9 (MYH9) and myosin light chain 9 (MYL9) by interacting with IQ-motif-containing GTPase-activating protein (IQGAP1). Consequently the lack of Arv1 delayed telophase-progression, and a strongly increased incidence of furrow regression and formation of multinuclear cells was observed both in human cells in culture and in follicle epithelial cells of egg chambers of Drosophila melanogaster in vivo. Interestingly, the cholesterol-status at the cleavage furrow did not affect the recruitment of either IQGAP1, MYH9 or MYL. These results identify a novel function for Arv1 in regulation of cell division through promotion of the contractile actomyosin ring, which is independent of its lipid transporter activity.

Epithelial protein lost in neoplasm (EPLIN): Beyond a tumor suppressor

“…Interestingly, EPLIN-β seems to have a stronger interaction with Arv1 when compared with the EPLIN-α isoform, suggesting the additional 160 aa at the N terminus may contribute to the physical association between the two proteins. 30 …”

Oligodendrocyte Progenitor Cells Increase Chi3l1 Secretion in exosome to Activate Myh9 and Promote Proliferation through Connexin47 Connected to Astrocytes

“…It also has angiogenesis, vascular remodeling abilities in vascular endothelial cells [66] and promotes tumor invasion, metastasis in some tumors [64,67]. Furthermore, Myh9 promotes tumor invasion and metastasis in some tumors [65,[68][69][70]. In addition, some studies have shown that Myh9 also contributes to cell proliferation, cell contraction, adhesion and cytokinesis.…”

A lipid regulator working at the cleavage furrow

“…Sundvold et al show that Arv1 becomes localized to the cell equator when the sister chromatids segregate into daughter cells during anaphase. 2 In early telophase, Arv1 is further enriched at the cleavage furrow and remains enriched until late telophase. This cell cycle-dependent localization of Arv1 raises the question whether Arv1 regulates assembly of the contractile ring.…”

“…In this volume of Cell Cycle, Sundvold et al, suggest that Arv1 is the protein that recruits myosin to the cleavage furrow by interacting with IQGAP1, a myosin-interacting IQ-motif-containing GTPase-activating protein. 2 Arv1 was originally identified as a protein essential for viability of budding yeast that lacks 2 acyl-coenzyme A cholesterol acyltransferase-related enzymes, Are1 and Are2. Arv1 is an endoplasmic reticulum (ER) membrane protein with multiple transmembrane domains and is conserved from yeast to human.…”

“…Next, Sundvold et al show that Arv1 not only interacts with EPLIN for its recruitment to the cleavage furrow, but it also interacts with myosin and IQGAP1. 2 Because Arv1 depletion reduces accumulation of myosin and IQGAP1 at the cleavage furrow, whereas depleting IQGAP1 does not affect accumulation of Arv1, the authors propose that Arv1 recruits myosin at the furrow by interacting with IQGAP1. Moreover, the authors show that Arv1 is dispensable for localization of F-actin and regulators of the contractile ring; RhoA, anillin, and that the Arv1-mediated recruitment of IQGAP1 or myosin is not dependent on cellular cholesterol levels, suggesting specific recruitment of myosin by a molecular pathway independent of RhoA, anillin and cholesterol (Fig.…”