AP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cells

Simple item page
dc.contributor.authorGravotta, Diego
dc.contributor.authorDeora, Ami
dc.contributor.authorPerret, Emilie
dc.contributor.authorOyanadel, Claudia
dc.contributor.authorSoza, Andrea
dc.contributor.authorSchreiner, Ryan
dc.contributor.authorRodriguez Boulan, Enrique
dc.date.accessioned2024-01-10T13:11:10Z
dc.date.available2024-01-10T13:11:10Z
dc.date.issued2007
dc.description.abstractThe epithelial-specific adaptor AP1B sorts basolateral proteins, but the trafficking routes where it performs its sorting role remain controversial. Here, we used an RNAi approach to knock down the medium subunit of AP1B (mu 1B) in the prototype epithelial cell line Madin-Darby canine kidney (MDCK). mu 1B-knocked down MDCK cells displayed loss of polarity of several endogenous and exogenous basolateral markers transduced via adenovirus vectors, but exhibited normal polarity of apical markers. We chose two well characterized basolateral protein markers, the transferrin receptor (TfR) and the vesicular stomatitis virus G protein, to study the sorting role of AP1B. A surface-capture assay introduced here showed that mu 1B-knocked down MDCK cells plated on filters at confluency and cultured for 4.5 d, sorted TfR correctly in the biosynthetic route but incorrectly in the recycling route. In contrast, these same cells missorted vesicular stomatitis virus G apically in the biosynthetic route. Strikingly, recently confluent MDCK cells (1-3 d) displayed AP1B-dependence in the biosynthetic route of TfR, which decreased with additional days in culture. Sucrose density gradient analysis detected AP1B predominantly in TfR-rich endosomal fractions in MDCK cells confluent for 1 and 4 d. Our results are consistent with the following model: AP1B sorts basolateral proteins in both biosynthetic and recycling routes of MDCK cells, as a result of its predominant functional localization in recycling endosomes, which constitute a post-Golgi station in the biosynthetic route of some plasma membrane proteins. TfR utilizes a direct route from Golgi to basolateral membrane that is established as the epithelial monolayer matures.
dc.description.funderNEI NIH HHS
dc.description.funderNIGMS NIH HHS
dc.description.funderNATIONAL EYE INSTITUTE
dc.description.funderNATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
dc.fechaingreso.objetodigital2024-05-06
dc.format.extent6 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1073/pnas.0610700104
dc.identifier.issn0027-8424
dc.identifier.pubmedidMEDLINE:17244703
dc.identifier.urihttps://doi.org/10.1073/pnas.0610700104
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/78006
dc.identifier.wosidWOS:000244081000024
dc.information.autorucMedicina;Gonzalez A;S/I;52306
dc.information.autorucMedicina;Soza A;S/I;129570
dc.issue.numero5
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final1569
dc.pagina.inicio1564
dc.publisherNATL ACAD SCIENCES
dc.revistaPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
dc.rightsacceso restringido
dc.subjectprotein sorting
dc.subjectclathrin adaptors
dc.subjectendosomes
dc.subjectpolarized secretion
dc.subjectepithelial cells
dc.subjectDARBY CANINE KIDNEY
dc.subjectPOLARIZED EPITHELIAL-CELLS
dc.subjectPOLYMERIC IMMUNOGLOBULIN RECEPTOR
dc.subjectINFLUENZA-VIRUS HEMAGGLUTININ
dc.subjectCLATHRIN ADAPTER COMPLEXES
dc.subjectMEMBRANE DOMAINS
dc.subjectENDOCYTIC PATHWAYS
dc.subjectCYTOPLASMIC DOMAIN
dc.subjectTARGETING SIGNAL
dc.subjectPLASMA-MEMBRANE
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cells
dc.typeartículo
dc.volumen104
sipa.codpersvinculados52306
sipa.codpersvinculados129570
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
2024-05-06. AP1B sorts basolateral proteins in recycling and biosynthetic routes of MDCK cells.pdf
Size:
3.35 KB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Artículos de revistas