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Precise Visualization of Insulin Receptors A and B in Murine Brain with an RNA In Situ Hybridization Assay
Published on: July 15, 2025
The insulin-like growth factor II/mannose-6-phosphate receptor : IGF-II/Man-6-P receptor
1Department of Biochemistry, University of Nebraska Medical Center, 42nd and Dewey Avenue, 68105-1065, Omaha, NE, USA.
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.
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