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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
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Nature Cell Biology
Article . 2000 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
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p95-APP1 links membrane transport to Rac-mediated reorganization of actin

Authors: DI CESARE A; PARIS S; ALBERTINAZZI C; DARIOZZI S; ANDERSEN J; MANN M; LONGHI R; +1 Authors

p95-APP1 links membrane transport to Rac-mediated reorganization of actin

Abstract

Motility requires protrusive activity at the cellular edge, where Rho family members regulate actin dynamics. Here we show that p95-APP1 (ArfGAP-putative, Pix-interacting, paxillin-interacting protein 1), a member of the GIT1/PKL family, is part of a complex that interacts with Rac. Wild-type and truncated p95-APP1 induce actin-rich protrusions mediated by Rac and ADP-ribosylation factor 6 (Arf6). Distinct p95-APP1-derived polypeptides have different distributions, indicating that p95-APP1 cycles between the cell surface and endosomes. Our results show that p95-APP1 functionally interacts with Rac and localizes to endosomal compartments, thus identifying p95-APP1 as a molecular link between actin organization, adhesion, and membrane transport during cell motility.

Keywords

Cells, Recombinant Fusion Proteins, Molecular Sequence Data, Fluorescent Antibody Technique, Cell Cycle Proteins, Chick Embryo, Endosomes, Models, Biological, Chromatography, Affinity, Models, Cell Movement, Cell Adhesion, Animals, Amino Acid Sequence, Cloning, Molecular, Cells, Cultured, Cytoskeleton, Adaptor Proteins, Signal Transducing, Chromatography, Cultured, ADP-Ribosylation Factors, GTPase-Activating Proteins, Cell Membrane, Signal Transducing, Adaptor Proteins, Molecular, Biological Transport, Fibroblasts, Biological, Phosphoproteins, Precipitin Tests, Actins, rac GTP-Binding Proteins, Molecular Weight, Enzyme Activation, Affinity, ADP-Ribosylation Factor 6, Guanosine Triphosphate, Carrier Proteins, Sequence Alignment, Cloning, Protein Binding

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    influence
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
120
Top 10%
Top 10%
Top 1%
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