High impact information on Ctbp2

• Finally, we found the RIBEYE homologue CtBP1 at ribbon and conventional synapses, suggesting a novel role for the CtBP/BARS family in the molecular assembly and function of central nervous system synapses [1].
• Molecular dissection of the photoreceptor ribbon synapse: physical interaction of Bassoon and RIBEYE is essential for the assembly of the ribbon complex [1].
• Our results suggest a model in which the nuclear localization of CtBP proteins is influenced by the CtBP2 NLS, by binding to PXDLS motif partner proteins, and through the effect of NADH on CtBP dimerization [2].
• Ctbp2-null mutation causes defects in axial patterning, heart morphogenesis and neural development [3].
• Surprisingly, however, this interaction with C-terminal-binding protein-2 is not required for FOG-2-mediated repression of GATA4-dependent transcription [4].

Biological context of Ctbp2

• The Ctbp2 mutant phenotype is more severe in the absence of Ctbp1 [3].
• Consistent with the known enzymatic activity of CtBP2, mutations at Arg272 in the substrate-binding domain and at His321 in the catalytic domain result in significant loss of CtBP2 transcriptional co-repressor activity [5].

Anatomical context of Ctbp2

• A direct interaction between the ribbon-specific protein RIBEYE and Bassoon seems to link the two compartments and is responsible for the physical integrity of the photoreceptor ribbon complex [1].

Other interactions of Ctbp2

• Ctbp1 mutant mice are small but viable and fertile, whereas Ctbp2-null mice show defects in axial patterning and die by E10.5 due to aberrant extraembryonic development [6].

Analytical, diagnostic and therapeutic context of Ctbp2

• In co-immunoprecipitation studies, calsenilin also interacted with CtBP1, a CtBP2 homolog [7].

References