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MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking.

Membrane-associated RING-CH (MARCH) is a recently identified member of the mammalian E3 ubiquitin ligase family, some members of which down-regulate the expression of immune recognition molecules. Here, we have identified MARCH-II, which is ubiquitously expressed and localized to endosomal vesicles and the plasma membrane. Immunoprecipitation and in vitro binding studies established that MARCH-II directly associates with syntaxin 6. Overexpression of MARCH-II resulted in redistribution of syntaxin 6 as well as some syntaxin-6-interacting soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) into the MARCH-II-positive vesicles. In addition, the retrograde transport of TGN38 and a chimeric version of furin to trans-Golgi network (TGN) was perturbed--without affecting the endocytic degradative and biosynthetic secretory pathways--similar to effects caused by a syntaxin 6 mutant lacking the transmembrane domain. MARCH-II overexpression markedly reduced the cell surface expression of transferrin (Tf) receptor and Tf uptake and interfered with delivery of internalized Tf to perinuclear recycling endosomes. Depletion of MARCH-II by small interfering RNA perturbed the TGN localization of syntaxin 6 and TGN38/46. MARCH-II is thus likely a regulator of trafficking between the TGN and endosomes, which is a novel function for the MARCH family.

Pubmed ID: 15689499


  • Nakamura N
  • Fukuda H
  • Kato A
  • Hirose S


Molecular biology of the cell

Publication Data

April 31, 2005

Associated Grants


Mesh Terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Cell Line
  • Cercopithecus aethiops
  • Cloning, Molecular
  • Cricetinae
  • Down-Regulation
  • Endosomes
  • Epidermal Growth Factor
  • Humans
  • Membrane Proteins
  • Molecular Sequence Data
  • Protein Binding
  • Protein Transport
  • Qa-SNARE Proteins
  • Rats
  • Receptor, Epidermal Growth Factor
  • Receptors, Transferrin
  • SNARE Proteins
  • Vesicular Transport Proteins
  • trans-Golgi Network