Neuroligin

Neurolign and neurexin "handshake"
Neuroligin
Tertiary structure of Neuroligin 4.[1]
Identifiers
SymbolNeuroligin
InterProIPR000460
Membranome72
neuroligin 1
Identifiers
SymbolNLGN1
NCBI gene22871
HGNC14291
OMIM600568
RefSeqNP_055747
UniProtQ8N2Q7
Other data
LocusChr. 3 q26.31
Search for
StructuresSwiss-model
DomainsInterPro
neuroligin 2
Identifiers
SymbolNLGN2
NCBI gene57555
HGNC14290
OMIM606479
RefSeqNP_065846
UniProtQ8NFZ4
Other data
LocusChr. 17 p13.1
Search for
StructuresSwiss-model
DomainsInterPro
neuroligin 3
Identifiers
SymbolNLGN3
NCBI gene54413
HGNC14289
OMIM300336
RefSeqNP_001160132
UniProtQ9NZ94
Other data
LocusChr. X q13.1
Search for
StructuresSwiss-model
DomainsInterPro
neuroligin 4X
Identifiers
SymbolNLGN4X
NCBI gene57502
HGNC14287
OMIM300427
RefSeqNP_065793
UniProtQ8N0W4
Other data
LocusChr. X p22.32-22.31
Search for
StructuresSwiss-model
DomainsInterPro

Neuroligin (NLGN), a type I membrane protein, is a cell adhesion protein on the postsynaptic membrane that mediates the formation and maintenance of synapses between neurons. Neuroligins act as ligands for β-neurexins, which are cell adhesion proteins located presynaptically. Neuroligin and β-neurexin "shake hands", resulting in the connection between two neurons and the production of a synapse.[2] Neuroligins also affect the properties of neural networks by specifying synaptic functions, and they mediate signalling by recruiting and stabilizing key synaptic components. Neuroligins interact with other postsynaptic proteins to localize neurotransmitter receptors and channels in the postsynaptic density as the cell matures.[3] Additionally, neuroligins are expressed in human peripheral tissues and have been found to play a role in angiogenesis.[4] In humans, alterations in genes encoding neuroligins are implicated in autism and other cognitive disorders.[5] Antibodies in a mother from previous male pregnancies against neuroligin 4 from the Y chromosome increase the probability of homosexuality in male offspring.

  1. ^ Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P (December 2007). "Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion". Neuron. 56 (6): 979–91. doi:10.1016/j.neuron.2007.11.013. PMC 2703725. PMID 18093521.
  2. ^ Scheiffele P, Fan J, Choih J, Fetter R, Serafini T (June 2000). "Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons". Cell. 101 (6): 657–69. doi:10.1016/S0092-8674(00)80877-6. PMID 10892652.
  3. ^ Cite error: The named reference Purves was invoked but never defined (see the help page).
  4. ^ Bottos A, Destro E, Rissone A, Graziano S, Cordara G, Assenzio B, Cera MR, Mascia L, Bussolino F, Arese M (December 2009). "The synaptic proteins neurexins and neuroligins are widely expressed in the vascular system and contribute to its functions". Proceedings of the National Academy of Sciences of the United States of America. 106 (49): 20782–7. Bibcode:2009PNAS..10620782B. doi:10.1073/pnas.0809510106. PMC 2791601. PMID 19926856.
  5. ^ Südhof TC (October 2008). "Neuroligins and neurexins link synaptic function to cognitive disease". Nature. 455 (7215): 903–11. Bibcode:2008Natur.455..903S. doi:10.1038/nature07456. PMC 2673233. PMID 18923512.