The insulin-like growth factor II/mannose-6-phosphate receptor - IGF-II/Man-6-P receptor

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Recent evidence from molecular cloning, biochemical and immunological experiments has established that the cation-independent mannose-6-phosphate (Man-6-P) receptor and insulin-like growth factor-II (IGF-II) receptor are the same protein. Although the role of the IGF-II/Man-6-P receptor as a transporter of hydrolytic enzymes in the biogenesis of lysosomes is certain, elucidation of the receptor's structure has not yet provided major insights into the function of IGF-II binding. Mutually exclusive binding of IGF-II and naturally occurring phosphomannosyl ligands to distinct but proximal sites on the receptor suggests that the IGF-II/Man-6-P receptor cannot simultaneously fulfill the functional requirements of both IGF-II and lysosomal enzymes. Does the receptor transduce on intracellular signal in order to mediate the biological effects of IGF-II? If so, then the receptor must interact with an effector molecule, perhaps a G protein, in the mechanism of IGF-II action. Further information from ligand binding and especially mutagenesis experiments will be needed to elucidate the potentially multiple functions of the IGF-II/Man-6-P receptor.

Original languageEnglish (US)
Pages (from-to)287-305
Number of pages19
JournalCytotechnology
Volume2
Issue number4
DOIs
StatePublished - Dec 1 1989

    Fingerprint

Keywords

  • IGF receptor
  • insulin-like growth factor-II
  • lysosomes
  • mannose-6-phosphate
  • protein sorting
  • signal transduction

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Clinical Biochemistry
  • Cell Biology

Cite this