v-SNARE cellubrevin is required for basolateral sorting of AP-1B-dependent cargo in polarized epithelial cells

Autor: Ian C. Fields, Heike Fölsch, Véronique Proux-Gillardeaux, Marc Pypaert, Thierry Galli, Elina Shteyn, Richard S. Kang
Přispěvatelé: Department of Biochemistry, Molecular Biology & Cell Biology Northwestern University, Department of Biochemistry, Molecular Biology & Cell Biology-Northwestern University, Department of Cell Biology [New Haven], Yale University School of Medicine-Howard Hughes Medical Institute (HHMI), Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (Avenir Program), the European Commission ('Signaling and Traffic' STREP 503229), the Association pour la Recherche sur le Cancer, the Ministère de la Recherche (ACI-BDP), the Fondation pour la Recherche Médicale, Yale University School of Medicine-Howard Hugues Medical Institute
Jazyk: angličtina
Rok vydání: 2007
Předmět:
Zdroj: Journal of Cell Biology
Journal of Cell Biology, Rockefeller University Press, 2007, 177 (3), pp.477-88. ⟨10.1083/jcb.200610047⟩
The Journal of Cell Biology
ISSN: 0021-9525
1540-8140
Popis: International audience; The epithelial cell-specific adaptor complex AP-1B is crucial for correct delivery of many transmembrane proteins from recycling endosomes to the basolateral plasma membrane. Subsequently, membrane fusion is dependent on the formation of complexes between SNARE proteins located at the target membrane and on transport vesicles. Although the t-SNARE syntaxin 4 has been localized to the basolateral membrane, the v-SNARE operative in the AP-1B pathway remained unknown. We show that the ubiquitously expressed v-SNARE cellubrevin localizes to the basolateral membrane and to recycling endosomes, where it colocalizes with AP-1B. Furthermore, we demonstrate that cellubrevin coimmunoprecipitates preferentially with syntaxin 4, implicating this v-SNARE in basolateral fusion events. Cleavage of cellubrevin with tetanus neurotoxin (TeNT) results in scattering of AP-1B localization and missorting of AP-1B-dependent cargos, such as transferrin receptor and a truncated low-density lipoprotein receptor, LDLR-CT27. These data suggest that cellubrevin and AP-1B cooperate in basolateral membrane trafficking.
Databáze: OpenAIRE