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Fig. 1. hGAR17 and hGAR22 isoforms and constructs. (A) hGAR17 mRNA and protein structure. The two mRNA splice forms differ from each other by the presence or absence of exon 2B and encode proteins with deduced molecular masses of 23.5 kDa (isoform {alpha}) and 96.5 kDa (isoform ß). Exon length in bp is indicated below each exon. hGAR17ß contains a calponin homology (CH) domain and a Gas2-related (GAR) domain. The amino acids comprising each domain are indicated. hGAR17{alpha} contains only a CH domain. The last 27 amino acids of hGAR17{alpha} (hatched box) are different from the corresponding sequence of hGAR17ß owing to a frameshift introduced into the {alpha} splice form by alternative splicing. The C-terminal sequence of hGAR17ß (C-tail 17) does not contain any known domains and is highly degenerate and unstructured. (B) hGAR17 constructs used in this study. All constructs contain a FLAG epitope tag at their N-terminus. The first and last amino acids of the hGAR17 sequence of each construct are indicated. (C) hGAR22 mRNA and protein structure. The two mRNA splice forms (see also Zucman-Rossi et al., 1996) differ from each other by the presence or absence of exon 5B and encode proteins with deduced molecular masses of 36.3 kDa (isoform {alpha}) and 72.6 kDa (isoform ß). Both isoforms contain a calponin homology (CH) domain and a Gas2-related (GAR) domain. The first 337 amino acids of hGAR22ß are identical to hGAR22{alpha}. The additional C-terminal sequence of hGAR22ß (C-tail 22) does not contain any known domains and appears to be highly degenerate and unstructured. (D) hGAR22 constructs used in this study.