Neuroligin: Difference between revisions
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<StructureSection load='' size='350' side='right' scene='42/422448/Cv/2' caption='Dimer of two mouse neuroligin-1 cholinesterase-like domains (magenta and cyan) in complex with two neurexin-beta1 LNS6 domains (salmon and yellow) and Ca+2 ions (green) [[3b3q]]'> | |||
== Function == | |||
[[Neuroligin|Neuroligins]] (NLGN) are a family of postsynaptic proteins which bind to the presynaptic [[Neurexin]] (NRXN) to form a complex which attaches neurons. In humans the NLGN family contains 4 to 5 members that are numbered 1, 2, 3, 4X and 5 or 4Y<ref>PMID:18093521</ref>. | |||
See [[Neurodevelopmental Disorders]]<br /> | |||
[[Neuroligin-Neurexin Interaction]] | |||
*'''NLGN-1''' regulates spines and synaptic plasticity<ref>PMID:26880202</ref>. <br /> | |||
*'''NLGN-2''' is localized to inhibitory synapses<ref>PMID:15540461</ref>. <br /> | |||
*'''NLGN-3''' is a synapse organizer which shapes normal function and autism disorder<ref>PMID:17897391</ref>. <br /> | |||
*'''NLGN-4''' is localized to glyceric post-synapses and regulates retina inhibition<ref>PMID:21282647</ref>. <br /> | |||
== Disease == | |||
Mutations in NLGN 4 are associated with autism and mental retardation<ref>PMID:19726642</ref>. | |||
== Structural insights == | |||
The <scene name='42/422448/Cv/5'>NLGN-NRXN complex involves the octahedrally coordinated Ca+2 ion</scene><ref>PMID:18084303</ref>. Water molecules are shown as red spheres. | |||
</StructureSection> | |||
== 3D Structures of Neuroligin == | == 3D Structures of Neuroligin == | ||
| Line 33: | Line 27: | ||
* Neuroligin | * Neuroligin | ||
**[[5ojk]] - hNLGN-1 cholinesterase domain - human<br /> | |||
**[[3bix]] - rNLGN-1 cholinesterase domain - rat<br /> | |||
**[[8gs4]] - hNLGN-2 – Cryo EM<br /> | |||
**[[3bl8]] - mNLGN-2 cholinesterase domain – mouse<br /> | **[[3bl8]] - mNLGN-2 cholinesterase domain – mouse<br /> | ||
**[[7cee]] - mNLGN-3 cholinesterase domain<br /> | |||
**[[3be8]] - hNLGN-4 cholinesterase domain – human<br /> | **[[3be8]] - hNLGN-4 cholinesterase domain – human<br /> | ||
* Neuroligin+neurexin | * Neuroligin+neurexin | ||
| Line 43: | Line 40: | ||
**[[3biw]] - rNLGN-1 cholinesterase domain+NRXN-1β LNS domain<br /> | **[[3biw]] - rNLGN-1 cholinesterase domain+NRXN-1β LNS domain<br /> | ||
**[[3vkf]] - rNLGN-1 cholinesterase domain + bNRXN-1β LNS domain | **[[3vkf]] - rNLGN-1 cholinesterase domain + bNRXN-1β LNS domain | ||
*NLGN other complexes | |||
**[[5oj6]] - rNLGN-1 cholinesterase domain + MDGA1<br /> | |||
**[[5v5v]] - rNLGN-2 cholinesterase domain + MDGA1<br /> | |||
**[[5xeq]] - rNLGN-2 cholinesterase domain (mutant) + MDGA1<br /> | |||
**[[7ceg]] - mNLGN-3 cholinesterase domain + PTP d<br /> | |||
}} | }} | ||
== References == | |||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 11:48, 13 July 2023
FunctionNeuroligins (NLGN) are a family of postsynaptic proteins which bind to the presynaptic Neurexin (NRXN) to form a complex which attaches neurons. In humans the NLGN family contains 4 to 5 members that are numbered 1, 2, 3, 4X and 5 or 4Y[1]. See Neurodevelopmental Disorders Neuroligin-Neurexin Interaction
DiseaseMutations in NLGN 4 are associated with autism and mental retardation[6]. Structural insightsThe [7]. Water molecules are shown as red spheres. |
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3D Structures of Neuroligin3D Structures of Neuroligin
13-July-2023
ReferencesReferences
- ↑ Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P. Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron. 2007 Dec 20;56(6):979-91. PMID:18093521 doi:10.1016/j.neuron.2007.11.013
- ↑ Liu A, Zhou Z, Dang R, Zhu Y, Qi J, He G, Leung C, Pak D, Jia Z, Xie W. Neuroligin 1 regulates spines and synaptic plasticity via LIMK1/cofilin-mediated actin reorganization. J Cell Biol. 2016 Feb 15;212(4):449-63. doi: 10.1083/jcb.201509023. PMID:26880202 doi:http://dx.doi.org/10.1083/jcb.201509023
- ↑ Varoqueaux F, Jamain S, Brose N. Neuroligin 2 is exclusively localized to inhibitory synapses. Eur J Cell Biol. 2004 Sep;83(9):449-56. PMID:15540461 doi:http://dx.doi.org/10.1078/0171-9335-00410
- ↑ Budreck EC, Scheiffele P. Neuroligin-3 is a neuronal adhesion protein at GABAergic and glutamatergic synapses. Eur J Neurosci. 2007 Oct;26(7):1738-48. doi: 10.1111/j.1460-9568.2007.05842.x. PMID:17897391 doi:http://dx.doi.org/10.1111/j.1460-9568.2007.05842.x
- ↑ Hoon M, Soykan T, Falkenburger B, Hammer M, Patrizi A, Schmidt KF, Sassoe-Pognetto M, Lowel S, Moser T, Taschenberger H, Brose N, Varoqueaux F. Neuroligin-4 is localized to glycinergic postsynapses and regulates inhibition in the retina. Proc Natl Acad Sci U S A. 2011 Feb 15;108(7):3053-8. doi:, 10.1073/pnas.1006946108. Epub 2011 Jan 31. PMID:21282647 doi:http://dx.doi.org/10.1073/pnas.1006946108
- ↑ Zhang C, Milunsky JM, Newton S, Ko J, Zhao G, Maher TA, Tager-Flusberg H, Bolliger MF, Carter AS, Boucard AA, Powell CM, Sudhof TC. A neuroligin-4 missense mutation associated with autism impairs neuroligin-4 folding and endoplasmic reticulum export. J Neurosci. 2009 Sep 2;29(35):10843-54. doi: 10.1523/JNEUROSCI.1248-09.2009. PMID:19726642 doi:http://dx.doi.org/10.1523/JNEUROSCI.1248-09.2009
- ↑ Chen X, Liu H, Shim AH, Focia PJ, He X. Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16. PMID:18084303 doi:10.1038/nsmb1350