The structure of cortical cytoplasm

Author:

Abstract

Actin-rich cortical cytoplasm of phagocytic leucocytes forms pseudopodia and controls cell shape and movement by generating directional propulsive and contractile forces. Proteins purified from leucocytes form and deform an actin matrix. Actinbinding protein (ABP) cross-links actin filaments into a three-dimensional lattice with perpendicular branches. This structure, which can be visualized in the electron microscope, is consistent with physical properties of actin-ABP matrices. Gelsolin binds one end of actin filaments with high affinity in the presence of calcium; acumentin, another protein, constitutively binds the other end with low affinity. Together these proteins can control actin filament length and thereby regulate expansion (propulsion) or collapse of the actin network. The assembly state of the network also controls myosin-based contractile forces. A tug-of-war decides the direction of lattice movement, regions of lesser structure tending to move toward regions of greater structure.

Publisher

The Royal Society

Subject

Industrial and Manufacturing Engineering,General Agricultural and Biological Sciences,General Business, Management and Accounting,Materials Science (miscellaneous),Business and International Management

Reference65 articles.

1. Regulation and Kinetics of the Actin-Myosin-ATP Interaction

2. The p and y cytoplasmic actins are differentially thermostabilized by MgADP; y actin binds MgADP more strongly. Biochem. biophys;Anderson N. L.;Res. Commun.,1979

3. Allison A. CL Davies P. & DePetris S. 1971 Role of contractile microfilaments in macrophage movement and endocytosis. Nature new Biol. 232 153-155.

4. Mechanico-chemical behaviour of F-actin. J. molec;Asakura S.;Biol.,1963

5. Interactions of actin, myosin, and an actin-binding protein of chronic myelogenous leukemia leukocytes.

Cited by 66 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

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