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Published online May 7, 2007
doi:10.1083/jcb.200610047
The Journal of Cell Biology, Vol. 177, No. 3, 477-488
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Fields et al.
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Article

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



Ian C. Fields1, Elina Shteyn1, Marc Pypaert2, Véronique Proux-Gillardeaux3, Richard S. Kang1, Thierry Galli3, and Heike Fölsch1

1 Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208
2 Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520
3 Institut National de la Santé et de la Recherche Médicale Avenir Team, Institut Jacques Monod, Unité Mixte de Recherche 7592, Centre National de la Recherche Scientifique, Universities Paris 6 and Paris 7, F-75005 Paris, Cedex 05, France

Correspondence to Heike Fölsch: h-folsch{at}northwestern.edu

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.

Abbreviations used in this paper: AP, adaptor protein; FcR, FcII-B2 receptor; LDLR, low-density lipoprotein receptor; TeNT, tetanus neurotoxin; TfnR, transferrin receptor; VAMP, vesicle-associated membrane protein; VSVG, vesicular stomatitis virus glycoprotein.


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