ARF1-mediated actin polymerization produces movement of artificial vesicles.

ARF1-mediated actin polymerization produces movement of artificial vesicles. Research Abstract Details 

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ARF1-mediated actin polymerization produces movement of artificial vesicles. Abstract Text:

Julien Heuvingh,Michel Franco,Philippe Chavrier, Sykes,

Vesicular trafficking and actin dynamics on Golgi membranes are both regulated by ADP-ribosylation factor 1 (ARF1) through the recruitment of various effectors, including vesicular coats. Actin assembly on Golgi membranes contributes to the architecture of the Golgi complex, vesicle formation, and trafficking and is mediated by ARF1 through a cascade that leads to Arp2/3 complex activation. Here we addressed the role of Golgi actin downstream of ARF1 by using a biomimetic assay consisting of liposomes of defined lipid composition, carrying an activated form of ARF1 incubated in cytosolic cell extracts. We observed actin polymerization around the liposomes resulting in thick actin shells and actin comet tails that pushed the ARF1 liposomes forward. The assay was used to characterize the ARF1-dependent pathway, leading to actin polymerization, and confirmed a dependency on CDC42 and its downstream effector N-WASP. Overall, this study demonstrates that actin polymerization driven by the complex multicomponent signaling cascade of the Golgi apparatus can be reproduced with a biomimetic system. Moreover, our results are consistent with the view that actin-based force generation at the site of vesicle formation contributes to the mechanism of fission. In addition to its well established function in coat recruitment, the ARF1 machinery also might produce movement- and fission-promoting forces through actin polymerization.

ARF1-mediated actin polymerization produces movement of artificial vesicles. Publishing Authors By Initials

J Heuvingh,M Franco,P Chavrier,C Sykes,

For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins: cdc42 gtp-binding protein research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: rho gtp-binding proteins: cdc42 gtp-binding protein research

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ARF1-mediated actin polymerization produces movement of artificial vesicles. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 16928-33

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 17

MONTH: 10

YEAR: 2007

ARF1-mediated actin polymerization produces movement of artificial vesicles. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7505876

ARF1-mediated actin polymerization produces movement of artificial vesicles. Keywords Mesh Terms:

KEYWORDS: cdc42 GTP-Binding Protein

MESH TERMS: metabolism

Chemical & Substance for Abstract: ARF1-mediated actin polymerization produces movement of artificial vesicles. Information

Substance Name: cdc42 GTP-Binding Protein

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for ARF1-mediated actin polymerization produces movement of artificial vesicles.

AFFILIATION: Centre de Recherche, Institut Curie, F-75248 Paris, France.

Country: United States

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MEDLINETA: Proc Natl Acad Sci U S A

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