Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography
| Autor: | Morten Nielsen, Hans Røigaard, Claus Munck Petersen, Linda Jacobsen, Niels Tommerup, Søren K. Moestrup, Anders Nykjaer, Hanne H. Rasmussen, Peder Madsen, Jørgen Gliemann |
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Complementary Endosome Recombinant Fusion Proteins Blotting Western Molecular Sequence Data Nerve Tissue Proteins Biochemistry Chromatography Affinity symbols.namesake Affinity chromatography Humans Amino Acid Sequence RNA Messenger Receptor Molecular Biology Furin Brain Chemistry Membrane Glycoproteins Microscopy Confocal biology Sequence Homology Amino Acid Endoplasmic reticulum Cell Biology Golgi apparatus Blotting Northern Adaptor Proteins Vesicular Transport LDL receptor symbols biology.protein Casein kinase 1 Sequence Alignment |
| Zdroj: | ResearcherID |
| Popis: | Receptor-associated protein (RAP) is an endoplasmic reticulum/Golgi protein involved in the processing of receptors of the low density lipoprotein receptor family. A approximately 95-kDa membrane glycoprotein, designated gp95/sortilin, was purified from human brain extracts by RAP affinity chromatography and cloned in a human cDNA library. The gene maps to chromosome 1p and encodes an 833-amino acid type I receptor containing an N-terminal furin cleavage site immediately preceding the N terminus determined in the purified protein. Gp95/sortilin is expressed in several tissues including brain, spinal cord, and testis. Gp95/sortilin is not related to the low density lipoprotein receptor family but shows intriguing homologies to established sorting receptors: a 140-amino acid lumenal segment of sortilin representing a hitherto unrecognized type of extracellular module shows extensive homology to corresponding segments in each of the two lumenal domains of yeast Vps10p, and the extreme C terminus of the cytoplasmic tail of sortilin contains the casein kinase phosphorylation consensus site and an adjacent dileucine sorting motif that mediate assembly protein-1 binding and lysosomal sorting of the mannose-6-phosphate receptors. Expression of a chimeric receptor containing the cytoplasmic tail of gp95/sortilin demonstrates evidence that the tail conveys colocalization with the cation-independent mannose6-phosphate receptor in endosomes and the Golgi compartment. |
| Databáze: | OpenAIRE |
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