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Figure 1


Fig. 1. Overview of the domain patterns of obscurin, Obsl1 and the C-terminal M-band-portion of titin. Key interaction sites between titin and obscurin/Obsl1 (above the domain pattern) and the positions of antibody epitopes (below the domain pattern) are marked. Also shown (in grey) are previously mapped interactions of obscurin with Z-disk titin and ankyrin, and M-band titin with MuRF, Nbr1, FHL2/DRAL and calpain-3 (CAPN3). The start of the alternative obscurin isoforms lacking the M-band-targeting motifs is shown. Signalling domains in obscurin include the Src homology domain (SH3), Dbl homology domain (DH) and pleckstrin homology domain (PH); DH and PH domains form a functional unit usually acting as a GDP-GTP exchange factor (GEF) of small G-proteins. Differentially spliced obscurin isoforms can also contain up to two protein kinase domains. The titin region deleted by the homozygous Mex3 mutation in Salih myopathy is marked.





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