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Beschreibung

Ankyrin repeat and sterile alpha motif domain-containing protein 1B (UniProt: P0C6S7, also known as Amyloid-beta protein intracellular domain-associated protein 1, AIDA-1, E2A-PBX1-associated protein, EB-1) is encoded by the Anks1b gene (Gene ID: 314721) in rat. AIDA-1 is an adaptor protein that has been implicated in Cajal body and nucleolar function. It is expressed throughout the brain and is highly expressed in the hippocampus. It is one of the most abundant proteins at postsynaptic densities where it is reported to bind to PSD95 and associates with NMDA receptors (NMDARs). In the brain, it interacts with amyloid b precursor protein and plays a role in brain development. AIDA-1 preferentially associates with GluN2B-containing NMDARs and plays a role in their transport from the endoplasmic reticulum (ER). Loss of AIDA-1 results in the accumulation of GluN2B in the ER and decreases GluN2B and increases GluN2A distribution at the synapse. However, loss of AIDA-1 does not affect AMPAR-mediated synaptic transmission or the probability of glutamate release. AIDA-1 has seven Ankyrin repeats in its N-terminal half and has two closely juxtaposed sterile alpha motif (SAM) domains (aa 810-876 and 884-949). Within the second SAM domain resides the nuclear localization signal (aa 935-938). Mutations in Anks1b gene are known to affect GluN2B function and are linked to the pathogenesis of neuropsychiatric disorders. (Ref.: Carbonell, AU., et al., (2019). Nat. Commun. 10(1), 3529, Tindi, JO., et al. (2015). J. Neurosci. 35(24), 8986- 8996).