The cytoplasmic tail of the cation-independent mannose 6-phosphate receptor contains four binding sites for AP-1

Pradipta Ghosh, Stuart Kornfeld

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

The trafficking of the cation-independent mannose 6-phosphate receptor between the trans-Golgi network and endosomes requires binding of sorting determinants in the cytoplasmic tail of the receptor to adaptor protein complex-1 (AP-1). Using a GST pull-down binding assay, four binding motifs were identified in the cytoplasmic tail: a tyrosine-based motif ( 26YSKV29), an internal dileucine-based motif ( 39ETEWLM44), and two casein kinase 2 sites ( 84DSEDE88 and 154DDSDED159). The YSKV motif mediated the strongest interaction with AP-1 and the two CK2 motifs bound AP-1 only when they were phosphorylated. The COOH-terminal dileucines were not required for interaction with AP-1.

Original languageEnglish
Pages (from-to)225-230
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume426
Issue number2
DOIs
StatePublished - Jun 15 2004

Keywords

  • AP-1
  • CI-MPR
  • Phosphorylation

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