Protein phosphatase 1 activity controls a balance between collective and single cell modes of migration

Author:

Chen Yujun1ORCID,Kotian Nirupama1,Aranjuez George2,Chen Lin3,Messer C Luke1,Burtscher Ashley2,Sawant Ketki1,Ramel Damien3ORCID,Wang Xiaobo3,McDonald Jocelyn A1ORCID

Affiliation:

1. Division of Biology, Kansas State University, Manhattan, United States

2. Lerner Research Institute, Cleveland Clinic, Cleveland, United States

3. LBCMCP, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, Toulouse, France

Abstract

Collective cell migration is central to many developmental and pathological processes. However, the mechanisms that keep cell collectives together and coordinate movement of multiple cells are poorly understood. Using the Drosophila border cell migration model, we find that Protein phosphatase 1 (Pp1) activity controls collective cell cohesion and migration. Inhibition of Pp1 causes border cells to round up, dissociate, and move as single cells with altered motility. We present evidence that Pp1 promotes proper levels of cadherin-catenin complex proteins at cell-cell junctions within the cluster to keep border cells together. Pp1 further restricts actomyosin contractility to the cluster periphery rather than at individual internal border cell contacts. We show that the myosin phosphatase Pp1 complex, which inhibits non-muscle myosin-II (Myo-II) activity, coordinates border cell shape and cluster cohesion. Given the high conservation of Pp1 complexes, this study identifies Pp1 as a major regulator of collective versus single cell migration.

Funder

National Institutes of Health

ARC Foundation for Cancer Research

National Science Foundation

Publisher

eLife Sciences Publications, Ltd

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience

Reference102 articles.

1. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase);Amano;Journal of Biological Chemistry,1996

2. The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes;Ambach;European Journal of Immunology,2000

3. Dynamic myosin activation promotes collective morphology and migration by locally balancing oppositional forces from surrounding tissue;Aranjuez;Molecular Biology of the Cell,2016

4. Ectopic expression of inhibitors of protein phosphatase type 1 (PP1) can be used to analyze roles of PP1 in Drosophila development;Bennett;Genetics,2003

5. Two distinct modes of guidance signalling during collective migration of border cells;Bianco;Nature,2007

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3