Identification of a Novel Mono-Leucine Basolateral Sorting Motif Within the Cytoplasmic Domain of Amphiregulin

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dc.contributor.authorGephart, Jonathan D.
dc.contributor.authorSingh, Bhuminder
dc.contributor.authorHigginbotham, James N.
dc.contributor.authorFranklin, Jeffrey L.
dc.contributor.authorGonzalez, Alfonso
dc.contributor.authorFoelsch, Heike
dc.contributor.authorCoffey, Robert J.
dc.date.accessioned2024-01-10T13:13:36Z
dc.date.available2024-01-10T13:13:36Z
dc.date.issued2011
dc.description.abstractEpithelial cells establish apical and basolateral (BL) membranes with distinct protein and lipid compositions. To achieve this spatial asymmetry, the cell utilizes a variety of mechanisms for differential sorting, delivery and retention of cell surface proteins. The EGF receptor (EGFR) and its ligand, amphiregulin (AREG), are transmembrane proteins delivered to the BL membrane in polarized epithelial cells. Herein, we show that the cytoplasmic domain of AREG (ACD) contains dominant BL sorting information; replacement of the cytoplasmic domain of apically targeted nerve growth factor receptor with the ACD redirects the chimera to the BL surface. Using sequential truncations and site-directed mutagenesis of the ACD, we identify a novel BL sorting motif consisting of a single leucine C-terminal to an acidic cluster (EEXXXL). In adaptor protein (AP)-1B-deficient cells, newly synthesized AREG is initially delivered to the BL surface as in AP-1B-expressing cells. However, in these AP-1B-deficient cells, recycling of AREG back to the BL surface is compromised, leading to its appearance at the apical surface. These results show that recycling, but not delivery, of AREG to the BL surface is AP-1B dependent.
dc.description.funderNCI
dc.description.funderBiochemical and Chemical Training for Cancer Research NCI
dc.description.funderNIH
dc.description.funderCONICYT
dc.description.funderEUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT
dc.description.funderEUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH &HUMAN DEVELOPMENT
dc.description.funderNATIONAL CANCER INSTITUTE
dc.description.funderNATIONAL EYE INSTITUTE
dc.description.funderNATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
dc.description.funderNATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
dc.fechaingreso.objetodigital2024-05-14
dc.format.extent12 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1111/j.1600-0854.2011.01282.x
dc.identifier.eissn1600-0854
dc.identifier.issn1398-9219
dc.identifier.pubmedidMEDLINE:21917092
dc.identifier.urihttps://doi.org/10.1111/j.1600-0854.2011.01282.x
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/78320
dc.identifier.wosidWOS:000297573500011
dc.information.autorucMedicina;Gonzalez A ;S/I;52306
dc.issue.numero12
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final1804
dc.pagina.inicio1793
dc.publisherWILEY
dc.revistaTRAFFIC
dc.rightsacceso restringido
dc.subjectmu 1B
dc.subjectamphiregulin
dc.subjectAP-1B
dc.subjectbasolateral
dc.subjectEGF receptor
dc.subjectLLC-PK1
dc.subjectMDCK
dc.subjectPOLARIZED EPITHELIAL-CELLS
dc.subjectCANINE KIDNEY-CELLS
dc.subjectGROWTH-FACTOR-ALPHA
dc.subjectMDCK CELLS
dc.subjectEGF RECEPTOR
dc.subjectMETALLOPROTEASE INHIBITOR
dc.subjectECTODOMAIN CLEAVAGE
dc.subjectMEMBRANE
dc.subjectPROTEINS
dc.subjectTYROSINE
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleIdentification of a Novel Mono-Leucine Basolateral Sorting Motif Within the Cytoplasmic Domain of Amphiregulin
dc.typeartículo
dc.volumen12
sipa.codpersvinculados52306
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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