MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II.

MARCH comprises a recently identified family of transmembrane RING-finger proteins which is implicated in diverse biological functions, such as immune regulation, protein quality control, and membrane trafficking. We previously identified MARCH-II, as a binding partner of syntaxin 6, which plays a role in endosomal protein transport. In this paper, we ...
describe the cloning and characterization of MARCH-III which is the closest homolog of MARCH-II. It is broadly expressed at relatively high levels in spleen, colon, and lung. An immunofluorescence study of HeLa cells demonstrated that MARCH-III is present in peripheral vesicles partially colocalized with transferrin receptor. Overexpression of MARCH-III resulted in the redistribution of TGN46 and strong inhibition of transferrin uptake. Immunoprecipitation studies revealed that MARCH-III is associated with syntaxin 6 and MARCH-II. Mutational analyses revealed that the PDZ-binding motif and RING finger are essential for the subcellular localization of MARCH-III and the inhibitory effect on transferrin uptake. The location, associated molecules, and effects of overexpression suggest that MARCH-III is involved in the regulation of vesicular trafficking in endosomes.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cloning, Molecular, DNA Primers, Endosomes, Fluorescent Antibody Technique, HeLa Cells, Humans, Immunoprecipitation, Membrane Proteins, Molecular Sequence Data, Rats, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid
J. Biochem.
Date: Jan. 01, 2006
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