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

EMBO J. 1993 May;12(5):2219-28.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Cells, Cultured
  • Cytoplasm / metabolism
  • Glycoproteins*
  • Golgi Apparatus / metabolism*
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism*
  • Membrane Proteins*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Sorting Signals / metabolism*
  • Rats
  • Sequence Deletion
  • Tyrosine / metabolism*

Substances

  • Glycoproteins
  • Membrane Glycoproteins
  • Membrane Proteins
  • Protein Sorting Signals
  • Tgoln2 protein, rat
  • Tyrosine