Antibody to AP1B adaptor blocks biosynthetic and recycling routes of basolateral proteins at recycling endosomes

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dc.contributor.authorCancino, Jorge
dc.contributor.authorTorrealba, Carolina
dc.contributor.authorSoza, Andrea
dc.contributor.authorYuseff, Maria Isabel
dc.contributor.authorGravotta, Diego
dc.contributor.authorHenklein, Peter
dc.contributor.authorRodriguez Boulan, Enrique
dc.contributor.authorGonzalez, Alfonso
dc.date.accessioned2024-01-10T13:45:57Z
dc.date.available2024-01-10T13:45:57Z
dc.date.issued2007
dc.description.abstractThe epithelial-specific adaptor AP1B sorts basolateral plasma membrane (PM) proteins in both biosynthetic and recycling routes, but the site where it carries out this function remains incompletely defined. Here, we have investigated this topic in Fischer rat thyroid (FRT) epithelial cells using an antibody against the medium subunit mu 1B. This antibody was suitable for immunofluorescence and blocked the function of AP1B in these cells. The antibody blocked the basolateral recycling of two basolateral PM markers, Transferrin receptor (TfR) and LDL receptor (LDLR), in a perinuclear compartment with marker and functional characteristics of recycling endosomes (RE). Live imaging experiments demonstrated that in the presence of the antibody two newly synthesized GFP-tagged basolateral proteins (vesicular stomatitis virus G [VSVG] protein and TfR) exited the trans-Golgi network (TGN) normally but became blocked at the RE within 3-5 min. By contrast, the antibody did not block trafficking of green fluorescent protein (GFP)-LDLR from the TGN to the PM but stopped its recycling after internalization into RE in similar to 45 min. Our experiments conclusively demonstrate that 1) AP1B functions exclusively at RE; 2) TGN-to-RE transport is very fast and selective and is mediated by adaptors different from AP1B; and 3) the TGN and AP1B-containing RE cooperate in biosynthetic basolateral sorting.
dc.description.funderNATIONAL EYE INSTITUTE
dc.description.funderNATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
dc.description.funderNEI NIH HHS
dc.description.funderNIGMS NIH HHS
dc.fechaingreso.objetodigital2024-04-30
dc.format.extent13 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1091/mbc.E07-06-0563
dc.identifier.eissn1939-4586
dc.identifier.issn1059-1524
dc.identifier.pubmedidMEDLINE:17881725
dc.identifier.urihttps://doi.org/10.1091/mbc.E07-06-0563
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/79100
dc.identifier.wosidWOS:000251660800018
dc.information.autorucMedicina;González A;S/I;52306
dc.information.autorucMedicina;Soza A;S/I;129570
dc.issue.numero12
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final4884
dc.pagina.inicio4872
dc.publisherAMER SOC CELL BIOLOGY
dc.revistaMOLECULAR BIOLOGY OF THE CELL
dc.rightsacceso restringido
dc.subjectPOLARIZED EPITHELIAL-CELLS
dc.subjectTRANS-GOLGI NETWORK
dc.subjectCANINE KIDNEY-CELLS
dc.subjectMDCK CELLS
dc.subjectPLASMA-MEMBRANE
dc.subjectSORTING SIGNALS
dc.subjectENDOCYTIC PATHWAYS
dc.subjectSTRUCTURAL REQUIREMENTS
dc.subjectTRANSFERRIN RECEPTOR
dc.subjectCOMMON ENDOSOMES
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAntibody to AP1B adaptor blocks biosynthetic and recycling routes of basolateral proteins at recycling endosomes
dc.typeartículo
dc.volumen18
sipa.codpersvinculados52306
sipa.codpersvinculados129570
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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