Splice variation in the cytoplasmic domains of myelin oligodendrocyte glycoprotein affects its cellular localisation and transport1

作者: Louise H. Boyle , James A. Traherne , Gemma Plotnek , Rosemary Ward , John Trowsdale

DOI: 10.1111/J.1471-4159.2007.04687.X

关键词:

摘要: Although myelin oligodendrocyte glycoprotein is a candidate autoantigen in multiple sclerosis, its function remains unknown. In humans, mRNA expressed by the gene alternatively spliced resulting at least nine unique protein isoforms. this study, we investigated sub-cellular localisation and membrane trafficking of six isoforms cloning them into mammalian expression vectors. Confocal microscopy revealed that these products are different cellular compartments. While two full-length (25.6 25.1) cell surface, three forms (22.7, 21.0 20.5) have more intracellular distribution, localising to endoplasmic reticulum and/or endosomes. Isoform 16.3, which lacks transmembrane domain, secreted. A switch may profound effects on receptor:ligand interactions consequently protein. The structural features alternative their differential, patterns could dictate exposure major immunogenic determinants within central nervous system. Our findings highlight splicing as factor be critical phenotypic sclerosis.

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