Author: ["Alessandra Di Cesare","Simona Paris","Chiara Albertinazzi","Simona Dariozzi","Jens Andersen","Matthias Mann","Renato Longhi","Ivan de Curtis"]
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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. Cite this article
Di Cesare, A., Paris, S., Albertinazzi, C. et al. p95-APP1 links membrane transport to Rac-mediated reorganization of actin . Nat Cell Biol 2, 521–530 (2000). https://doi.org/10.1038/35019561 