2005
DOI: 10.1074/jbc.m406797200
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The V-ATPase Subunit C Binds to Polymeric F-actin as Well as to Monomeric G-actin and Induces Cross-linking of Actin Filaments

Abstract: Previously, we have shown that the V-ATPase holoenzyme as well as the V 1 complex isolated from the midgut of the tobacco hornworm (Manduca sexta) exhibits the ability of binding to actin filaments via the V 1 subunits B and C (Vitavska, O., Wieczorek, H., and Merzendorfer, H. (2003) J. Biol. Chem. 278, 18499 -18505). Since the recombinant subunit C not only enhances actin binding of the V 1 complex but also can bind separately to F-actin, we analyzed the interaction of recombinant subunit C with actin. We dem… Show more

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Cited by 97 publications
(93 citation statements)
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“…29 Bundling can be assayed by low speed sedimentation since cross-linked bundles of F-actin readily pellet, whereas single actin filaments remain in solution. 30 To determine if lamin A tails bundled F-actin, we polymerized purified G-actin (7.9 µM), then incubated 1 hour with each tested tail polypeptide (6.7 µM) at a molar ratio of ~1:1 (actin monomer to tail monomer), and centrifuged at 17,000 g, resolved pellets by SDS-PAGE, stained with GelCode Blue (Fig. 3A, B and D), and quantified by densitometry ( Fig.…”
Section: Resultsmentioning
confidence: 99%
“…29 Bundling can be assayed by low speed sedimentation since cross-linked bundles of F-actin readily pellet, whereas single actin filaments remain in solution. 30 To determine if lamin A tails bundled F-actin, we polymerized purified G-actin (7.9 µM), then incubated 1 hour with each tested tail polypeptide (6.7 µM) at a molar ratio of ~1:1 (actin monomer to tail monomer), and centrifuged at 17,000 g, resolved pellets by SDS-PAGE, stained with GelCode Blue (Fig. 3A, B and D), and quantified by densitometry ( Fig.…”
Section: Resultsmentioning
confidence: 99%
“…This indicates that a significant portion of these subunits is not assembled with B2 and that they may be associated with the cytoskeleton by an alternate linkage. One possibility is that these subunits are associated with the C-subunit, which is thought to bind microfilaments when V-ATPases are not fully assembled (43)(44)(45).…”
Section: Discussionmentioning
confidence: 99%
“…21 Furthermore, in view of the observation that the (pro)renin receptor equals a subunit of the V-ATPase complex, 28 V-ATPase transport might be responsible for the reorganization of actin cytoskeleton. 35 In fact, V-ATPase-induced acidosis is sufficient to activate p38 MAPK and HSP27. 36,37 …”
Section: Discussionmentioning
confidence: 99%