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      The Actin Cytoskeleton and Actin-Based Motility

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      Journal: Cold Spring Harbor Perspectives in Biology
      Publisher: Cold Spring Harbor Laboratory

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          Abstract

          <p id="d720118e90">The actin cytoskeleton—a collection of actin filaments with their accessory and regulatory proteins—is the primary force-generating machinery in the cell. It can produce pushing (protrusive) forces through coordinated polymerization of multiple actin filaments or pulling (contractile) forces through sliding actin filaments along bipolar filaments of myosin II. Both force types are particularly important for whole-cell migration, but they also define and change the cell shape and mechanical properties of the cell surface, drive the intracellular motility and morphogenesis of membrane organelles, and allow cells to form adhesions with each other and with the extracellular matrix. </p>

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          Editorial

          Robert Aune, Matthew Taliaferro, Adam Sage … (2000)
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            Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner.

            Colin Choi, Miguel Vicente-Manzanares, Jessica Zareno … (2008)
            Using two-colour imaging and high resolution TIRF microscopy, we investigated the assembly and maturation of nascent adhesions in migrating cells. We show that nascent adhesions assemble and are stable within the lamellipodium. The assembly is independent of myosin II but its rate is proportional to the protrusion rate and requires actin polymerization. At the lamellipodium back, the nascent adhesions either disassemble or mature through growth and elongation. Maturation occurs along an alpha-actinin-actin template that elongates centripetally from nascent adhesions. Alpha-Actinin mediates the formation of the template and organization of adhesions associated with actin filaments, suggesting that actin crosslinking has a major role in this process. Adhesion maturation also requires myosin II. Rescue of a myosin IIA knockdown with an actin-bound but motor-inhibited mutant of myosin IIA shows that the actin crosslinking function of myosin II mediates initial adhesion maturation. From these studies, we have developed a model for adhesion assembly that clarifies the relative contributions of myosin II and actin polymerization and organization.
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              Defining macropinocytosis.

              Markus Kerr, Rohan Teasdale (2009)
              Macropinocytosis represents a distinct pathway of endocytosis in mammalian cells. This actin-driven endocytic process is not directly co-ordinated by the presence of cargo but can be induced upon activation of growth factor signalling pathways. The capacity to dissect the contribution of macropinocytosis to cellular processes has been hampered by a lack of unique molecular markers and defining features. While aspects of macropinosome formation and maturation are common to those shared by the other endocytic pathways, a number of key differences have recently begun to emerge and will be discussed in this study. It is now well established that macropinocytosis significantly contributes to antigen presentation by the immune system and is exploited by a range of pathogens for cellular invasion and avoidance of immune surveillance.
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                Author and article information

                Journal
                Title: Cold Spring Harbor Perspectives in Biology
                Abbreviated Title: Cold Spring Harb Perspect Biol
                Publisher: Cold Spring Harbor Laboratory
                ISSN (Electronic): 1943-0264
                Publication date Created: January 02 2018
                Publication date (Electronic): January 02 2018
                Publication date (Print): January 2018
                Volume: 10
                Issue: 1
                Page: a018267
                Article
                DOI: 10.1101/cshperspect.a018267
                PMC ID: 5749151
                PubMed ID: 29295889
                SO-VID: a72e7026-c0fa-4aff-878b-728c87cdb144
                Copyright © © 2018
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