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

Stöckli, Jacqueline; Höning, Stefan; Rohrer, Jack

doi:10.1074/jbc.M313525200

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	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
Authors:	Stöckli, Jacqueline Höning, Stefan Rohrer, Jack
DOI:	10.1074/jbc.M313525200
Published in:	Journal of Biological Chemistry
Volume(Issue):	279
Issue:	22
Page(s):	23542
Pages to:	23549
Issue Date:	28-May-2004
Publisher / Ed. Institution:	American Society for Biochemistry and Molecular Biology
ISSN:	1083-351X
Language:	English
Subject (DDC):	572: Biochemistry
Abstract:	Lysosomal 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.
URI:	https://digitalcollection.zhaw.ch/handle/11475/6815
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:	Publikationen Life Sciences und Facility Management

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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.