Abstract
Originalsprog | Engelsk |
---|---|
Tidsskrift | Journal of Biological Chemistry |
Vol/bind | 272 |
Udgave nummer | 6 |
Sider (fra-til) | 3599-605 |
Antal sider | 6 |
ISSN | 0021-9258 |
Status | Udgivet - 1997 |
Udgivet eksternt | Ja |
Bibliografisk note
Keywords: Amino Acid Sequence; Blotting, Northern; Blotting, Western; Brain Chemistry; Chromatography, Affinity; DNA, Complementary; Humans; Membrane Glycoproteins; Microscopy, Confocal; Molecular Sequence Data; Nerve Tissue Proteins; RNA, Messenger; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino AcidCitationsformater
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Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography. / Petersen, C M; Nielsen, M S; Nykjaer, A; Rasmussen, H H; Roigaard, H; Gliemann, J; Madsen, P; Moestrup, S K; Tommerup, Niels.
I: Journal of Biological Chemistry, Bind 272, Nr. 6, 1997, s. 3599-605.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography.
AU - Petersen, C M
AU - Nielsen, M S
AU - Nykjaer, A
AU - Rasmussen, H H
AU - Roigaard, H
AU - Gliemann, J
AU - Madsen, P
AU - Moestrup, S K
AU - Tommerup, Niels
N1 - Keywords: Amino Acid Sequence; Blotting, Northern; Blotting, Western; Brain Chemistry; Chromatography, Affinity; DNA, Complementary; Humans; Membrane Glycoproteins; Microscopy, Confocal; Molecular Sequence Data; Nerve Tissue Proteins; RNA, Messenger; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid
PY - 1997
Y1 - 1997
N2 - 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.
AB - 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.
M3 - Journal article
C2 - 9013611
VL - 272
SP - 3599
EP - 3605
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 6
ER -