High impact information on GJA9

• However, until now in vivo phosphorylation of Cx36 has not been reported [1].
• AII amacrine cells express the gap junctional protein connexin36 (Cx36) [1].
• Our results link increased phosphorylation of Cx36 to down-regulation of permeability through gap junction channels mediating light adaptation in the retina [1].
• Though cyclic GMP and calcium did not greatly influence the association of these proteins with connexin 36, the results suggest the possibility of connexin 36 associating with other proteins [2].

Biological context of GJA9

• Connexin 36 in bovine retina: lack of phosphorylation but evidence for association with phosphorylated proteins [2].
• Though all the connexins involved in light adaptation and information transfer from rod to cone pathway are not yet known, connexin 36 has been shown to be definitively involved in the latter process [2].

Anatomical context of GJA9

• Together, these observations indicate that interneuronal communication at gap junctions made by connexin 36 may not be regulated by direct phosphorylation of connexin 36, but possibly by phosphorylation of associated proteins [2].
• Phosphorylation of Cx36 has been hypothesized to regulate gap junctional activity of AII amacrine cells [1].

Analytical, diagnostic and therapeutic context of GJA9

• Immunoprecipitation did reveal phosphorylated proteins coimmunoprecipitated with connexin 36 [2].

References