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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 RIS Download

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

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