Functions of CELF proteins Sample Clauses

Functions of CELF proteins. Members of CELF protein family are involved in several post-transcriptional events including: regulation of alternative splicing, translation and mRNA localisation (Xxxxxxxxx et al., 1996) (Xxxxxxxx et al., 2001) (Xxxxx and Xxxxxxxx, 2010; Xxxx et al., 2005). The divergent domain of CELF4 is implicated in splicing activity of some specific pre-mRNA targets. These include promotion of cardiac troponin T (cTNT) exon 5 inclusion, PTB exon 11 inclusion and NDMA R1 (N-Methyl-D-aspartate receptor 1) exon 5 exclusion (Xxxxx et al., 2004). Similarly, the divergent domain of CELF2 plays a role in alternative splicing of CFTR (cystic-fibrosis trans- membrane conductance regulator) exon 9 (Xxxxxxxx et al., 2010). CELF3 is a unique CELF protein with a 15-18 polyglutamine (polyQ) repeat in its divergent domain encoded by variable CAG repeats (Figure 1.10) (Xxxxxxx et al., 2007; Xxxxx and Xxxxxxxx, 2010; Xxxxxxxx et al., 1997). CELF3 was originally identified by a screen of candidate disease genes in cDNA libraries containing CAG repeats encoding long polyQ tracts (Xxxxxxxx et al., 1997). As a result of this polyQ tract, CELF3 is also known as TNRC4 (tri-nucleotide repeat containing 4). Some neurological disorders caused by CAG repeat expansion, include Huntington’s disease (HD) and spinocerebellar ataxia type 1 (SCA1) (Xxxxxxxxxxx and Xxxxxxxxxx, 2003) (Suzuki et al., 2008). It is unlikely that the polyQ tract in CELF3 tract will be the subject to pathogenic expansion, because it does not have a high degree of variation within the human population (Xxxxxxx et al., 2007). As a result, CELF3 is not associated with any polyglutamine expansion disorders. This is because proteins with repeat CAG lengths of about 40 or more are sequestered into aggregates (Xxxx and Xxxxxxx, 2011). For instance in HD, CAG triplet repeat expansion in Huntingtin (HTT) gene leads to pathogenic expanded polyQ stretch in HTT protein (Xxx et al., 2004; Xxxx and Xxxxxxx, 2011). Moreover, co-expressed CELF3 was not recruited into cytoplasmic huntingtin aggregates or nuclear aggregates of ataxin-1 in CHO cells (Xxxxxxx et al., 2007).
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