Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor

Y. Zhu, B. Doray, A. Poussu, V. P. Lehto, S. Kornfeld

Research output: Contribution to journalArticlepeer-review

233 Scopus citations

Abstract

The GGAs are a multidomain protein family implicated in protein trafficking between the Golgi and endosomes. Here, the VHS domain of GGA2 was shown to bind to the acidic cluster-dileucine motif in the cytoplasmic tail of the cation-independent mannose 6-phosphate receptor (CI-MPR). Receptors with mutations in this motif were defective in lysosomal enzyme sorting. The hinge domain of GGA2 bound clathrin, suggesting that GGA2 could be a link between cargo molecules and clathrin-coated vesicle assembly. Thus, GGA2 binding to the CI-MPR is important for lysosomal enzyme targeting.

Original languageEnglish
Pages (from-to)1716-1718
Number of pages3
JournalScience
Volume292
Issue number5522
DOIs
StatePublished - Jun 1 2001

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