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PMID: 7479735 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Biosynthetic transport of the asialoglycoprotein receptor H1 to the cell surface occurs via endosomes.

Leitinger B, Hille-Rehfeld A, Spiess M

Abstract

Signals for endocytosis and for basolateral and lysosomal sorting are closely related in a number of membrane proteins, suggesting similar sorting mechanisms at the plasma membrane and in the trans-Golgi network (TGN). We tested the hypothesis that basolateral membrane proteins are transported to the cell surface via endosomes for the asialoglycoprotein receptor H1. This protein was tagged with a tyrosine sulfation site (H1TS) to allow specific labeling with [35S]sulfate in the TGN. Madin-Darby canine kidney cells expressing H1TS were pulse-labeled and chased for a period of time insufficient for labeled H1TS to reach the cell surface. Upon homogenization and gradient centrifugation, fractions devoid of TGN were subjected to immunoisolation of compartments containing mannose 6-phosphate receptor, which served as an endosomal marker. H1TS in transit to the cell surface was efficiently coisolated, whereas a labeled secretory protein and free glycosaminoglycan chains were not. This indicates an indirect pathway for the asialoglycoprotein receptor to the plasma membrane via endosomes and has important implications for protein sorting in the TGN and endosomes.

MeSH Terms
Animals Asialoglycoprotein Receptor Asialoglycoproteins/metabolism Cell Line Cell Membrane/metabolism Dogs Endocytosis Endosomes/metabolism Glycosaminoglycans/isolation & purification,metabolism Golgi Apparatus/metabolism Kidney Kinetics Lysosomes/metabolism Receptor, IGF Type 2/metabolism Receptors, Cell Surface/biosynthesis,isolation & purification,metabolism Sulfates/metabolism Sulfur Radioisotopes
Chemicals
Asialoglycoprotein Receptor Asialoglycoproteins Glycosaminoglycans Receptor, IGF Type 2 Receptors, Cell Surface Sulfates Sulfur Radioisotopes
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Leitinger B
Department of Biochemistry, Biozentrum, University of Basel, Switzerland.
Hille-Rehfeld A
Spiess M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1995-10-24
Pages
10109-13
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC40745
Subset
IM
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