a decrease in editing at the Q/R site.ADAR1 double knockouts have no effect on editing. Structure The edited adenosine is located in the 22 immunogloulin like repeat of the protein. This region is an integrin β binding domain and a RAC1 binding domain. The amino acid change is likely to effect the electrostatic potential of the binding domains. FLNA editing site is 2 nucleotides from a splice site like the R/G site of GluR-2. Both transcripts have 7/8 identical nucleotides around their editing sites. Since it is widely thought that editing at the GLUR-2 Q/R site influences splicing, the sequence and editing site similarity could mean that editing at the FLNA site could also regulate splicing. In vitro experiments of gluR-2 have shown that presence of ADAR2 results in inhibition of splicing. Analysis of EST data for FLNA show that there is a link between editing of the last exon codon and retention of the following intron. Function The change in electrostatic potential is likely to effect the binding of FLNA to the many proteins it interacts with. DNA repair Interaction of FLNA with the BRCA1 protein is required for efficient regulation of early stages of DNA repair processes. FLNA is implicated in the control of the DNA repair process of homologous recombination and non-homologous end joining. References Further reading External links GeneReview/NCBI/NIH/UW entry on Otopalatodigital Spectrum Disorders GeneReviews/NIH/NCBI/UW entry on X-Linked Periventricular Heterotopia or Bilateral Periventricular Nodular Heterotopia de:Filamin