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Polarized transport requires AP-1-mediated recruitment of KIF13A and KIF13B at the trans-Golgi.
Montgomery, Andrew C; Mendoza, Christina S; Garbouchian, Alex; Quinones, Geraldine B; Bentley, Marvin.
Afiliación
  • Montgomery AC; Department of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180.
  • Mendoza CS; Department of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180.
  • Garbouchian A; Department of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180.
  • Quinones GB; Department of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180.
  • Bentley M; Department of Biological Sciences and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180.
Mol Biol Cell ; 35(5): ar61, 2024 May 01.
Article en En | MEDLINE | ID: mdl-38446634
ABSTRACT
Neurons are polarized cells that require accurate membrane trafficking to maintain distinct protein complements at dendritic and axonal membranes. The Kinesin-3 family members KIF13A and KIF13B are thought to mediate dendrite-selective transport, but the mechanism by which they are recruited to polarized vesicles and the differences in the specific trafficking role of each KIF13 have not been defined. We performed live-cell imaging in cultured hippocampal neurons and found that KIF13A is a dedicated dendrite-selective kinesin. KIF13B confers two different transport modes, dendrite- and axon-selective transport. Both KIF13s are maintained at the trans-Golgi network by interactions with the heterotetrameric adaptor protein complex AP-1. Interference with KIF13 binding to AP-1 resulted in disruptions to both dendrite- and axon-selective trafficking. We propose that AP-1 is the molecular link between the sorting of polarized cargoes into vesicles and the recruitment of kinesins that confer polarized transport.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cinesinas / Red trans-Golgi / Complejo 1 de Proteína Adaptadora / Aparato de Golgi Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cinesinas / Red trans-Golgi / Complejo 1 de Proteína Adaptadora / Aparato de Golgi Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos