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J Cell Sci. 2017 Oct 15;130(20):3427-3435. doi: 10.1242/jcs.206433.

Actin assembly mechanisms at a glance.

Author information

1
Division of Molecular Cell Biology, Zoological Institute, Technische Universit├Ąt Braunschweig, 38106 Braunschweig, Germany.
2
Department of Cell Biology, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany.
3
Institute for Biophysical Chemistry, Hannover Medical School, 30625 Hannover, Germany.
4
Institute for Physiology and Pathophysiology, Department of Molecular Cell Physiology, Philipps-University of Marburg, 35032 Marburg, Germany.
5
Institute for Medical Microbiology, Virology and Hygiene, University Medical Center Eppendorf, 20246 Hamburg, Germany.
6
Department of Neurology, University Hospital Regensburg, 93053 Regensburg, Germany Eugen.Kerkhoff@ukr.de.

Abstract

The actin cytoskeleton and associated motor proteins provide the driving forces for establishing the astonishing morphological diversity and dynamics of mammalian cells. Aside from functions in protruding and contracting cell membranes for motility, differentiation or cell division, the actin cytoskeleton provides forces to shape and move intracellular membranes of organelles and vesicles. To establish the many different actin assembly functions required in time and space, actin nucleators are targeted to specific subcellular compartments, thereby restricting the generation of specific actin filament structures to those sites. Recent research has revealed that targeting and activation of actin filament nucleators, elongators and myosin motors are tightly coordinated by conserved protein complexes to orchestrate force generation. In this Cell Science at a Glance article and the accompanying poster, we summarize and discuss the current knowledge on the corresponding protein complexes and their modes of action in actin nucleation, elongation and force generation.

KEYWORDS:

Actin cytoskeleton; Actin filament elongation; Actin nucleation; Membrane contractions; Membrane protrusion; Membrane trafficking; Myosin force generation; Rho-GTPase signalling

PMID:
29032357
DOI:
10.1242/jcs.206433
[Indexed for MEDLINE]
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