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A more recent version of this article appeared on April 1, 2003
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Submitted on July 17, 2002
Revised on October 31, 2002
Accepted on December 26, 2002
1 Cell Adhesion Unit, Department of Molecular Biology and Functional Genomics - DIBIT, S. Raffaele Scientific Institute, Via Olgettina 58, 20132 Milano, Italy
* Corresponding author. E-mail address: decurtis.ivan{at}hsr.it.
The mechanisms coordinating adhesion, actin organization, and membrane traffic during growth cone migration are poorly understood. Neuritogenesis and branching from retinal neurons are regulated by the Rac1B/Rac3 GTPase. We have identified a functional connection between Arf6 and p95-APP1 during the regulation of Rac1B-mediated neuritogenesis. P95-APP1 is an ArfGAP of the GIT family expressed in the developing nervous system. We show that Arf6 has a predominant role in neurite extension when compared to Arf1 and Arf5. Cotransfection experiments indicate a specific and cooperative potentiation of neurite extension by Arf6 and the carboxyterminal portion of p95-APP1. Localization studies in neurons expressing different p95-derived constructs show a codistribution of p95-APP1 with Arf6, but not Arf1. Moreover, p95-APP1-derived proteins with a mutated or deleted ArfGAP domain prevent Rac1B-induced neuritogenesis, leading to PIX-mediated accumulation at large Rab11-positive endocytic vesicles. Our data support a role of p95-APP1 as a specific regulator of Arf6 in the control of membrane trafficking during neuritogenesis.
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