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PMID: 8194522 Published · ppublish English Journal Article

Retrieval of TGN proteins from the cell surface requires endosomal acidification.

The EMBO journal ·Vol. 13 ·No. 10 ·1994-05-15 ·Pages 2305-12

Chapman RE, Munro S

Abstract

TGN38 is a protein of unknown function located in the trans-Golgi network (TGN) of mammalian cells. Its intracellular distribution is maintained by it being continuously retrieved from the plasma membrane. In this paper we show that when cells are treated with agents such as chloroquine which neutralize acidic organelles, the movement of TGN38 along the endocytic pathway is blocked. The same effect is observed with a second TGN protein, the protease furin. We show that the cytoplasmic tail of furin is sufficient to confer a chloroquine-sensitive TGN localization on a heterologous protein. These results imply that the internal pH of endosomes affects sorting processes mediated by signals in the cytoplasmic portion of proteins and have implications for the role of acidification in endosomal function.

MeSH Terms
Acids/metabolism Amino Acid Sequence Animals Biological Transport/drug effects Cell Compartmentation Cell Membrane/metabolism Chloroquine/pharmacology Endocytosis/drug effects,physiology Fluorescent Antibody Technique Furin Glycoproteins Golgi Apparatus/enzymology,metabolism Membrane Glycoproteins/metabolism Membrane Proteins Molecular Sequence Data Organelles/metabolism Subtilisins/metabolism
Chemicals
Acids Glycoproteins Membrane Glycoproteins Membrane Proteins Chloroquine Subtilisins Furin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Chapman R E
MRC Laboratory of Molecular Biology, Cambridge, UK.
Munro S
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1994-05-15
Pages
2305-12
Language
English
Region
England
NLM ID
8208664
PMCID
PMC395094
Subset
IM
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