P-type lectins. Biochim Biophys Acta 2002 Sep 19;1572(2-3):317-40
Date
09/12/2002Pubmed ID
12223278DOI
10.1016/s0304-4165(02)00317-3Scopus ID
2-s2.0-0037136418 (requires institutional sign-in at Scopus site) 196 CitationsAbstract
The two members of the P-type lectin family, the cation-dependent mannose 6-phosphate receptor (CD-MPR) and the insulin-like growth factor II/mannose 6-phosphate receptor (IGF-II/MPR), are distinguished from all other lectins by their ability to recognize phosphorylated mannose residues. The P-type lectins play an essential role in the generation of functional lysosomes within the cells of higher eukaryotes by directing newly synthesized lysosomal enzymes bearing the mannose 6-phosphate (M6P) signal to lysosomes. At the cell surface, the IGF-II/MPR also binds to the nonglycosylated polypeptide hormone, IGF-II, targeting this potent mitogenic factor for degradation in lysosomes. Moreover, in recent years, the multifunctional nature of the IGF-II/MPR has become increasingly apparent, as the list of extracellular ligands recognized by this receptor has grown to include a diverse spectrum of M6P-containing proteins as well as nonglycosylated ligands, implicating a role for the IGF-II/MPR in a number of important physiological pathways. Recent investigations have provided valuable insights into the molecular basis of ligand recognition by the MPRs as well as the complex intracellular trafficking pathways traversed by these receptors. This review provides a current view on the structures, functions, and medical relevance of the P-type lectins.
Author List
Dahms N, Hancock MKAuthor
Nancy M. Dahms PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Crystallography
Endoplasmic Reticulum
Endosomes
Golgi Apparatus
Humans
Lectins
Ligands
Lysosomes
Membrane Glycoproteins
Models, Molecular
Molecular Sequence Data
Receptor, IGF Type 2
Sequence Alignment
