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PMID: 8491209 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

TGN38 is maintained in the trans-Golgi network by a tyrosine-containing motif in the cytoplasmic domain.

The EMBO journal ·Vol. 12 ·No. 5 ·1993-05-00 ·Pages 2219-28

Bos K, Wraight C, Stanley KK

Abstract

Sorting of proteins destined for different plasma membrane domains, lysosomes and secretory pathways takes place in the trans-Golgi network (TGN). TGN38 is an integral membrane protein found in this intracellular compartment. We show that TGN38 contains an autonomous targeting signal within its cytoplasmic domain which determines its intracellular location. Deletion analysis and site-directed mutagenesis of this domain demonstrate that a tyrosine motif homologous to the internalization signal of surface receptors is necessary and sufficient for correct localization. These findings suggest that TGN38 is maintained in the TGN by retrieval from the plasma membrane and employs a different mechanism for retention from that of the transferase enzymes of the trans-Golgi.

MeSH Terms
Amino Acid Sequence Animals Biological Transport Cells, Cultured Cytoplasm/metabolism Glycoproteins Golgi Apparatus/metabolism Membrane Glycoproteins/genetics,metabolism Membrane Proteins Molecular Sequence Data Mutagenesis, Site-Directed Protein Sorting Signals/metabolism Rats Sequence Deletion Tyrosine/metabolism
Chemicals
Glycoproteins Membrane Glycoproteins Membrane Proteins Protein Sorting Signals Tgoln2 protein, rat Tyrosine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bos K
Heart Research Institute, Camperdown, NSW, Sydney, Australia.
Wraight C
Stanley K K
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1993-05-00
Pages
2219-28
Language
English
Region
England
NLM ID
8208664
PMCID
PMC413443
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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