Rottner, Klemens and Faix, Jan and Bogdan, Sven and Linder, Stefan and Kerkhoff, Eugen (2017) Actin assembly mechanisms at a glance. JOURNAL OF CELL SCIENCE, 130 (20). pp. 3427-3435. ISSN 0021-9533, 1477-9137
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | WISKOTT-ALDRICH-SYNDROME; FILAMENT BARBED-END; PRIMARY HUMAN MACROPHAGES; FOCAL ADHESION FORMATION; SYNDROME PROTEIN WASP; ARP2/3 COMPLEX; N-WASP; FILOPODIA FORMATION; STRESS FIBERS; CELL-MIGRATION; Actin cytoskeleton; Actin nucleation; Actin filament elongation; Myosin force generation; Membrane protrusion; Membrane contractions; Membrane trafficking; Rho-GTPase signalling |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Neurologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Dec 2018 13:19 |
| Last Modified: | 01 Mar 2019 08:19 |
| URI: | https://pred.uni-regensburg.de/id/eprint/2006 |
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