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dc.contributor.authorStöckli, Jacqueline-
dc.contributor.authorHöning, Stefan-
dc.contributor.authorRohrer, Jack-
dc.date.accessioned2018-06-13T08:53:19Z-
dc.date.available2018-06-13T08:53:19Z-
dc.date.issued2004-05-28-
dc.identifier.issn1083-351Xde_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/6815-
dc.description.abstractLysosomal biogenesis depends on proper transport of lysosomal enzymes by the cation-dependent mannose 6-phosphate receptor (CD-MPR) from the trans-Golgi network (TGN) to endosomes. Trafficking of the CDMPR is mediated by sorting signals in its cytoplasmic tail. GGA1 (Golgi-localizing, gamma-ear-containing, ARF-binding protein-1) binds to CD-MPR in the TGN and targets the receptor to clathrin-coated pits for transport from the TGN to endosomes. The motif of the CD-MPR that interacts with GGA1 was shown to be 61DXXLL65. Reports on increased affinity of cargo, when phosphorylated by casein kinase 2 (CK2), to GGAs focused our interest on the effect of the CD-MPR CK2 site on binding to GGA1. Here we demonstrate that Glu58 and Glu59 of the CK2 site are essential for high affinity GGA1 binding in vitro, whereas the phosphorylation of Ser57 of the CD-MPR has no influence on receptor binding to GGA1. Furthermore, the in vivo interaction between GGA1 and CD-MPR was abolished only when all residues involved in GGA1 binding were mutated, namely, Glu58, Glu59, Asp61, Leu64, and Leu65. In contrast, the binding of adaptor protein-1 (AP-1) to CD-MPR required all the glutamates surrounding the phosphorylation site, namely, Glu55, Glu56, Glu58, and Glu59, but like GGA1 binding, was independent of the phosphorylation of Ser57. The binding affinity of GGA1 to the CD-MPR was found to be 2.4-fold higher than that of AP-1. This could regulate the binding of the two proteins to the partly overlapping sorting signals, allowing AP-1 binding to the CD-MPR only when GGA1 is released upon autoinhibition by phosphorylation.de_CH
dc.language.isoende_CH
dc.publisherAmerican Society for Biochemistry and Molecular Biologyde_CH
dc.relation.ispartofJournal of Biological Chemistryde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleThe acidic cluster of the CK2 site of the cation-dependent mannose 6-phosphate receptor (CD-MPR) but not its phosphorylation is required for GGA1 and AP-1 bindingde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
zhaw.organisationalunitInstitut für Chemie und Biotechnologie (ICBT)de_CH
dc.identifier.doi10.1074/jbc.M313525200de_CH
zhaw.funding.euNode_CH
zhaw.issue22de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.end23549de_CH
zhaw.pages.start23542de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume279de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedZellphysiologiede_CH
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Stöckli, J., Höning, S., & Rohrer, J. (2004). The acidic cluster of the CK2 site of the cation-dependent mannose 6-phosphate receptor (CD-MPR) but not its phosphorylation is required for GGA1 and AP-1 binding. Journal of Biological Chemistry, 279(22), 23542–23549. https://doi.org/10.1074/jbc.M313525200
Stöckli, J., Höning, S. and Rohrer, J. (2004) ‘The acidic cluster of the CK2 site of the cation-dependent mannose 6-phosphate receptor (CD-MPR) but not its phosphorylation is required for GGA1 and AP-1 binding’, Journal of Biological Chemistry, 279(22), pp. 23542–23549. Available at: https://doi.org/10.1074/jbc.M313525200.
J. Stöckli, S. Höning, and J. Rohrer, “The acidic cluster of the CK2 site of the cation-dependent mannose 6-phosphate receptor (CD-MPR) but not its phosphorylation is required for GGA1 and AP-1 binding,” Journal of Biological Chemistry, vol. 279, no. 22, pp. 23542–23549, May 2004, doi: 10.1074/jbc.M313525200.
STÖCKLI, Jacqueline, Stefan HÖNING und Jack ROHRER, 2004. The acidic cluster of the CK2 site of the cation-dependent mannose 6-phosphate receptor (CD-MPR) but not its phosphorylation is required for GGA1 and AP-1 binding. Journal of Biological Chemistry. 28 Mai 2004. Bd. 279, Nr. 22, S. 23542–23549. DOI 10.1074/jbc.M313525200
Stöckli, Jacqueline, Stefan Höning, and Jack Rohrer. 2004. “The Acidic Cluster of the CK2 Site of the Cation-Dependent Mannose 6-Phosphate Receptor (CD-MPR) but Not Its Phosphorylation Is Required for GGA1 and AP-1 Binding.” Journal of Biological Chemistry 279 (22): 23542–49. https://doi.org/10.1074/jbc.M313525200.
Stöckli, Jacqueline, et al. “The Acidic Cluster of the CK2 Site of the Cation-Dependent Mannose 6-Phosphate Receptor (CD-MPR) but Not Its Phosphorylation Is Required for GGA1 and AP-1 Binding.” Journal of Biological Chemistry, vol. 279, no. 22, May 2004, pp. 23542–49, https://doi.org/10.1074/jbc.M313525200.


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