Changes of the actin filament system in the green algaMicrasterias denticulata induced by different cytoskeleton inhibitors

PROTOPLASMA ◽  
2000 ◽  
Vol 212 (3-4) ◽  
pp. 206-216 ◽  
Author(s):  
M. Pfl�gl-Haill ◽  
L. Vidali ◽  
J. W. Vos ◽  
P. K. Hepler ◽  
U. L�tz-Meindl
Keyword(s):  
Actin Filament ◽  
Filament System

Structure-Function Studies of the Actin Filament System of Acanthamoeba

1989 ◽  
pp. 271-279
Author(s):  
Thomas D. Pollard ◽  
Karen A. Magnus ◽  
Stephen Doberstein ◽  
Pascal Goldschmidt-Clermont ◽  
Donald A. Kaiser ◽  
...  
Keyword(s):  
Structure Function ◽  
Actin Filament ◽  
Filament System

Regulation of adherens junction protein p120ctnby 10 nM CCK precedes actin breakdown in rat pancreatic acini

2000 ◽  
Vol 278 (3) ◽  
pp. G486-G491 ◽  
Author(s):  
J. Leser ◽  
M. F. Beil ◽  
O. A. Musa ◽  
G. Adler ◽  
M. P. Lutz
Keyword(s):  
Tyrosine Phosphorylation ◽  
Actin Filament ◽  
Adherens Junctions ◽  
Adherens Junction ◽  
Acinar Cells ◽  
Pancreatic Acini ◽  
Filament System ◽  
Adherens Junction Protein ◽  
Junction Protein ◽  
E Cadherin

The initial pathophysiological events that characterize CCK-hyperstimulation pancreatitis include the breakdown of the actin filament system and disruption of cadherin-catenin protein complexes. Cadherins and catenins are part of adherens junctions, which may act as anchor for the cellular actin filament system. We examined the composition and regulation of adherens junctions during CCK-induced acinar cell damage. Freshly isolated CCK-stimulated rat pancreatic acini were examined for actin filaments and functional adherens junctions by immunocytology and laser confocal scanning microscopy or by coprecipitation and immunoblotting for E-cadherin, β- and α-catenin, p120ctn, and phosphotyrosine. In addition to E-cadherin and β-catenin, acinar cells express the cadherin-regulatory protein p120ctn and the attachment protein α-catenin. Both colocalize and coimmunoprecipitate with E-cadherin in one complex, and all colocalize with the terminal actin web. Supramaximal secretory CCK concentrations (10 nM) initiated tyrosine phosphorylation of p120ctn but not of β-catenin within 2 min, preceding the breakdown of the terminal actin web by several minutes. Under these conditions, the cadherin-catenin association within the adherens junction complex remained intact. We describe for the first time supramaximal CCK-dependent tyrosine phosphorylation of the adherens junction protein p120ctnand demonstrate the presence of an intact adherens junction protein complex in acinar cells. p120ctn may participate in the actin filament breakdown during experimental conditions mimicking pancreatitis.

scholarly journals The Intrinsic GDP/GTP Exchange Activities of Cdc42 and Rac1 Are Critical Determinants for Their Specific Effects on Mobilization of the Actin Filament System

Cells ◽  
2019 ◽  
Vol 8 (7) ◽  
pp. 759 ◽  
Author(s):  
Pontus Aspenström
Keyword(s):  
Actin Filament ◽  
Rho Gtpases ◽  
Focal Adhesions ◽  
Small Gtpases ◽  
Migration And Invasion ◽  
Actin Nucleation ◽  
Filament System ◽  
Prevailing Paradigm ◽  
Specific Effects ◽  
Cytoskeletal Dynamics

The Rho GTPases comprise a subfamily of the Ras superfamily of small GTPases. Their importance in regulation of cell morphology and cell migration is well characterized. According to the prevailing paradigm, Cdc42 regulates the formation of filopodia, Rac1 regulates the formation of lamellipodia, and RhoA triggers the assembly of focal adhesions. However, this scheme is clearly an oversimplification, as the Rho subfamily encompasses 20 members with diverse effects on a number of vital cellular processes, including cytoskeletal dynamics and cell proliferation, migration, and invasion. This article highlights the importance of the catalytic activities of the classical Rho GTPases Cdc42 and Rac1, in terms of their specific effects on the dynamic reorganization of the actin filament system. GTPase-deficient mutants of Cdc42 and Rac1 trigger the formation of broad lamellipodia and stress fibers, and fast-cycling mutations trigger filopodia formation and stress fiber dissolution. The filopodia response requires the involvement of the formin family of actin nucleation promotors. In contrast, the formation of broad lamellipodia induced by GTPase-deficient Cdc42 and Rac1 is mediated through Arp2/3-dependent actin nucleation.

The BRG1 and the Actin Filament System

2006 ◽  
pp. 135-162
Author(s):  
Ann‐Kristin Östlund Farrants ◽  
Erica Cavellán ◽  
Patrik Asp
Keyword(s):  
Actin Filament ◽  
Filament System
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