Abstract
Synaptic adhesion molecules are known to participate in various steps of synapse development including initial contacts between dendrites and axons, formation of early synapses, and their maturation and plastic changes. Notably, a significant subset of synaptic adhesion molecules associates with synaptic scaffolding proteins, suggesting that they may act in concert to couple trans-synaptic adhesion to molecular organization of synaptic proteins. Here, we describe an emerging group of synaptic adhesion molecules that directly interact with the abundant postsynaptic scaffold PSD-95, which include neuroligins, NGLs, SALMs, and ADAM22, and discuss how these proteins and PSD-95 act together to regulate synaptic development. PSD-95 may be one of the central organizers of synaptic adhesion that recruits diverse proteins to sites of synaptic adhesion, promotes trans-synaptic signaling, and couples neuronal activity with changes in synaptic adhesion.
| Original language | English |
|---|---|
| Pages (from-to) | 263-283 |
| Number of pages | 21 |
| Journal | Progress in Neurobiology |
| Volume | 84 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 2008 Mar 1 |
| Externally published | Yes |
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Keywords
- ADAM22
- Netrin-G
- Neurexin
- Neuroligin
- NGL
- PSD-95
- SALM
- Synapse
ASJC Scopus subject areas
- Neuroscience(all)
Cite this
Synaptic adhesion molecules and PSD-95. / Han, Kihoon; Kim, Eunjoon.
In: Progress in Neurobiology, Vol. 84, No. 3, 01.03.2008, p. 263-283.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Synaptic adhesion molecules and PSD-95
AU - Han, Kihoon
AU - Kim, Eunjoon
PY - 2008/3/1
Y1 - 2008/3/1
N2 - Synaptic adhesion molecules are known to participate in various steps of synapse development including initial contacts between dendrites and axons, formation of early synapses, and their maturation and plastic changes. Notably, a significant subset of synaptic adhesion molecules associates with synaptic scaffolding proteins, suggesting that they may act in concert to couple trans-synaptic adhesion to molecular organization of synaptic proteins. Here, we describe an emerging group of synaptic adhesion molecules that directly interact with the abundant postsynaptic scaffold PSD-95, which include neuroligins, NGLs, SALMs, and ADAM22, and discuss how these proteins and PSD-95 act together to regulate synaptic development. PSD-95 may be one of the central organizers of synaptic adhesion that recruits diverse proteins to sites of synaptic adhesion, promotes trans-synaptic signaling, and couples neuronal activity with changes in synaptic adhesion.
AB - Synaptic adhesion molecules are known to participate in various steps of synapse development including initial contacts between dendrites and axons, formation of early synapses, and their maturation and plastic changes. Notably, a significant subset of synaptic adhesion molecules associates with synaptic scaffolding proteins, suggesting that they may act in concert to couple trans-synaptic adhesion to molecular organization of synaptic proteins. Here, we describe an emerging group of synaptic adhesion molecules that directly interact with the abundant postsynaptic scaffold PSD-95, which include neuroligins, NGLs, SALMs, and ADAM22, and discuss how these proteins and PSD-95 act together to regulate synaptic development. PSD-95 may be one of the central organizers of synaptic adhesion that recruits diverse proteins to sites of synaptic adhesion, promotes trans-synaptic signaling, and couples neuronal activity with changes in synaptic adhesion.
KW - ADAM22
KW - Netrin-G
KW - Neurexin
KW - Neuroligin
KW - NGL
KW - PSD-95
KW - SALM
KW - Synapse
UR - http://www.scopus.com/inward/record.url?scp=39249084254&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=39249084254&partnerID=8YFLogxK
U2 - 10.1016/j.pneurobio.2007.10.011
DO - 10.1016/j.pneurobio.2007.10.011
M3 - Review article
C2 - 18206289
AN - SCOPUS:39249084254
VL - 84
SP - 263
EP - 283
JO - Progress in Neurobiology
JF - Progress in Neurobiology
SN - 0301-0082
IS - 3
ER -