New Insights into Mechanism and Regulation of Actin Capping Protein

Cooper, John A.; Sept, David

doi:10.1016/s1937-6448(08)00604-7

Cited by 206 publications

(263 citation statements)

References 91 publications

(124 reference statements)

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“…The CAPZ dimer binds barbed ends of actin filaments to prevent further elongation. Through this effect CAPZ controls filament length and branch density, and consequently force generation at areas of Arp2/3-mediated actin assembly (10). CAPZ was also recently shown to indirectly promote filament nucleation by Arp2/3 complex by shifting the balance of VCA activity from filament barbed end binding (28) to promotion of nucleation (29).…”

Section: Resultsmentioning

confidence: 97%

WASH and WAVE actin regulators of the Wiskott–Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes

Jia

Gomez

Metlagel

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

207

325

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We recently showed that the Wiskott-Aldrich syndrome protein (WASP) family member, WASH, localizes to endosomal subdomains and regulates endocytic vesicle scission in an Arp2/3-dependent manner. Mechanisms regulating WASH activity are unknown. Here we show that WASH functions in cells within a 500 kDa core complex containing Strumpellin, FAM21, KIAA1033 (SWIP), and CCDC53. Although recombinant WASH is constitutively active toward the Arp2/3 complex, the reconstituted core assembly is inhibited, suggesting that it functions in cells to regulate actin dynamics through WASH. FAM21 interacts directly with CAPZ and inhibits its actin-capping activity. Four of the five core components show distant (approximately 15% amino acid sequence identify) but significant structural homology to components of a complex that negatively regulates the WASP family member, WAVE. Moreover, biochemical and electron microscopic analyses show that the WASH and WAVE complexes are structurally similar. Thus, these two distantly related WASP family members are controlled by analogous structurally related mechanisms. Strumpellin is mutated in the human disease hereditary spastic paraplegia, and its link to WASH suggests that misregulation of actin dynamics on endosomes may play a role in this disorder.actin dynamics and capping | endosome | WAVE regulatory complex | WASH regulatory complex | hereditary spastic paraplegia

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Section: Resultsmentioning

confidence: 97%

WASH and WAVE actin regulators of the Wiskott–Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes

Jia

Gomez

Metlagel

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

207

325

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“…Clmn and nck-associated protein 1 (Nckap1) (14) are actin binding IMPs. Actin-related protein 2/3 complex subunit 2/4 (Arpc2 and Arpc4) (15), gelsolin isoform 2 (Gsn) (16), adseverin isoform-1 (Scin) (17)(18)(19), and filamentous actin (F-actin) capping protein β (Capzb) (20) are F-actin end-binding proteins. Mpp5 (21,22), drebrin-like protein isoform 3 (Dbn1) (23)(24)(25), and LIM and SH3 domain protein 1 (Lasp1) (26) are actinbinding adaptor proteins.…”

Section: Quantitative Analysis Of the Apical Plasma Membrane Proteome Inmentioning

confidence: 99%

Quantitative apical membrane proteomics reveals vasopressin-induced actin dynamics in collecting duct cells

Loo

Chen

Wang

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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In kidney collecting duct cells, filamentous actin (F-actin) depolymerization is a critical step in vasopressin-induced trafficking of aquaporin-2 to the apical plasma membrane. However, the molecular components of this response are largely unknown. Using stable isotope-based quantitative protein mass spectrometry and surface biotinylation, we identified 100 proteins that showed significant abundance changes in the apical plasma membrane of mouse cortical collecting duct cells in response to vasopressin. Fourteen of these proteins are involved in actin cytoskeleton regulation, including actin itself, 10 actin-associated proteins, and 3 regulatory proteins. Identified were two integral membrane proteins (Clmn, Nckap1) and one actin-binding protein (Mpp5) that link F-actin to the plasma membrane, five F-actin end-binding proteins (Arpc2, Arpc4, Gsn, Scin, and Capzb) involved in F-actin reorganization, and two actin adaptor proteins (Dbn1, Lasp1) that regulate actin cytoskeleton organization. There were also protease (Capn1), protein kinase (Cdc42bpb), and Rho guanine nucleotide exchange factor 2 (Arhgef2) that mediate signal-induced F-actin changes. Based on these findings, we devised a live-cell imaging method to observe vasopressininduced F-actin dynamics in polarized mouse cortical collecting duct cells. In response to vasopressin, F-actin gradually disappeared near the center of the apical plasma membrane while consolidating laterally near the tight junction. This F-actin peripheralization was blocked by calcium ion chelation. Vasopressin-induced apical aquaporin-2 trafficking and forskolin-induced water permeability increase were blocked by F-actin disruption. In conclusion, we identified a vasopressin-regulated actin network potentially responsible for vasopressin-induced apical F-actin dynamics that could explain regulation of apical aquaporin-2 trafficking and water permeability increase.V asopressin regulates aquaporin-2 (AQP2) and osmotic water transport in the collecting duct by regulating total AQP2 protein abundance and AQP2 trafficking to and from the apical plasma membrane of principal cells (1). Understanding these regulatory mechanisms at the molecular level is important to the ultimate understanding of the pathophysiology of multiple water balance disorders (2). This goal is abetted by the methods of molecular systems biology (proteomics and transcriptomics), which not only reveal "parts lists" for collecting duct cells but also can identify what biological and molecular processes are regulated by vasopressin. These proteomic and transcriptomic data have been made publicly available in databases (3). Many of these studies have focused on whole cells (4-6), whereas several analyzed subcellular fractions (7-12). Analysis of subcellular fractions is technically demanding, but it has the benefit of identifying low abundance proteins with important functions. To identify proteins potentially involved in apical AQP2 trafficking, we previously used NHS-based surface biotinylation coupled to streptavidin...

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“…Also, the analysis of chromatographic fractions and polymerization kinetic indicated the presence of trace amounts of an active factor in "natural" mussel actin, whose molecular weight is somewhat higher than the actin weight. This factor most likely is similar to the capping protein (CP), which is a heterodimer with a molecular weight of about 60 kDa [20]. Earlier, the actin-capping activity was found in the residue of acetone powder, after extraction of actin [21].…”

Section: Discussionmentioning

confidence: 91%

Natural Actin and Tropomyosin from Molluscan Catch Muscle

Uv¹,

Ss²,

Ig³

et al. 2017

J Phys Chem Biophys

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New Insights into Mechanism and Regulation of Actin Capping Protein

Cited by 206 publications

References 91 publications

WASH and WAVE actin regulators of the Wiskott–Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes

WASH and WAVE actin regulators of the Wiskott–Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes

Quantitative apical membrane proteomics reveals vasopressin-induced actin dynamics in collecting duct cells

Natural Actin and Tropomyosin from Molluscan Catch Muscle

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