calsyntenin-3; alcadein-beta; alc-beta (CLSTN3 CS3 KIAA0726)
Jump to navigation
Jump to search
Function
- may modulate Ca+2-mediated postsynaptic signals
- complex formation with APBA2 & APP
- stabilizes APP metabolism & enhances APBA2-mediated suppression of beta-APP40 secretion, due to retardation of intracellular APP maturation
- proteolytically processed under normal cellular conditions
- primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (salc) & a short C-terminal transmembrane fragment (CTF1)
- secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-alc-beta chain in the extracellular milieu & produces an intracellular fragment (alcICD). this processing is strongly suppressed in the tripartite complex formed with APBA2 & APP, which seems to prevent the association with gamma-secretase
- directly interacts with APBA2. forms a tripartite complex with APBA2 & APP
- interacts with low affinity with KLC1
Structure
- binds synaptic Ca+2 with its cytoplasmic domain
- contains 2 cadherin domains
Compartment
- cell membrane; single-pass type 1 membrane protein (putative)
- endoplasmic reticulum membrane
- Golgi membrane
- most prominent in the postsynaptic specializations of asymmetric (type 1) synapses with both axodendritic & axospinous localization (putative)
Expression
- expressed predominantly in the brain & in kidney
- low levels in heart, skeletal muscle, liver, placenta, pancreas & lung[2]
- predominant expression inbrain, & only marginal in kidney[3]
- in brain, present throughout all cortical layers
- highest levels in GABAergic neurons (based on morphology & distribution pattern)
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/Q9BQT9.html
- ↑ 2.0 2.1 Hintsch G et al The calsyntenins--a family of postsynaptic membrane proteins with distinct neuronal expression patterns. Mol Cell Neurosci. 2002 Nov;21(3):393-409. PMID: https://www.ncbi.nlm.nih.gov/pubmed/12498782
- ↑ 3.0 3.1 Araki Y et al Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta- protein precursor metabolism. J Biol Chem. 2003 Dec 5;278(49):49448-58. Epub 2003 Sep 12. PMID: https://www.ncbi.nlm.nih.gov/pubmed/12972431