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

Arch Biochem Biophys. 2004 Jun 15;426(2):225-30. doi: 10.1016/j.abb.2004.02.011.

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 ((26)YSKV(29)), an internal dileucine-based motif ((39)ETEWLM(44)), and two casein kinase 2 sites ((84)DSEDE(88) and (154)DDSDED(159)). 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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Protein Complex 1 / chemistry*
  • Adaptor Protein Complex 1 / metabolism*
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Binding Sites
  • Cytoplasm / chemistry*
  • Cytoplasm / metabolism*
  • Phosphorylation
  • Protein Binding
  • Receptor, IGF Type 2 / chemistry*
  • Receptor, IGF Type 2 / metabolism*
  • Structure-Activity Relationship

Substances

  • Adaptor Protein Complex 1
  • Receptor, IGF Type 2