Sjoegren syndrome nuclear autoantigen 1 (SSNA1/NA14) is a major specific target for autoantibodies in Sjögren's Syndrome, a highly prevalent autoimmune disease [1, 2]. NA14 localises specifically to centrioles and may act as an adaptor protein regulating spastin (a microtubule-severing protein) localisation to centrosomes. NA14 can assemble into large fibrils, a structure that is important for its interaction with spastin as well as for microtubule dynamics [3]. It is also a binding partner for the G-protein coupled receptor TPRA40, which regulates early mouse embryogenesis [4].
Orthologues of SSNA1 are absent from the common eukaryotic model systems Saccharomyces cerevisiae, Caenorhabditis elegans and Drosophila melanogaster but are encoded by the genomes of the flagellated green alga Chlamydomonas reinhardtii (where it is known as deflagellation-inducible protein of 13 kDa, DIP13), trematode worms and protozoan parasites. Chlamydomonas reinhardtii DIP13 is localised to centrioles, flagella and cytoplasmic microtubules. It is involved in cell division and flagellar assembly [5, 6].
1. NA14 is a novel nuclear autoantigen with a coiled-coil domain. J. Biol. Chem. 273, 1634-9
2. Autoantibody to NA14 is an independent marker primarily for Sjogren's syndrome. Front Biosci (Landmark Ed) 14, 3733-9
3. Spastin-interacting protein NA14/SSNA1 functions in cytokinesis and axon development. PLoS ONE 9, e112428
4. TPRA40/GPR175 regulates early mouse embryogenesis through functional membrane transport by Sjogren's syndrome-associated protein NA14. J. Cell. Physiol. 217, 194-206
5. Chlamydomonas DIP13 and human NA14: a new class of proteins associated with microtubule structures is involved in cell division. J. Cell. Sci. 116, 1449-62
6. GFP as a tool for the analysis of proteins in the flagellar basal apparatus of Chlamydomonas. Cell Motil. Cytoskeleton 61, 189-200
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