RGD Reference Report - Selected SALM (synaptic adhesion-like molecule) family proteins regulate synapse formation. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Selected SALM (synaptic adhesion-like molecule) family proteins regulate synapse formation.

Authors: Mah, Won  Ko, Jaewon  Nam, Jungyong  Han, Kihoon  Chung, Woo Suk  Kim, Eunjoon 
Citation: Mah W, etal., J Neurosci. 2010 Apr 21;30(16):5559-68. doi: 10.1523/JNEUROSCI.4839-09.2010.
RGD ID: 13702463
Pubmed: (View Article at PubMed) PMID:20410109
DOI: Full-text: DOI:10.1523/JNEUROSCI.4839-09.2010

Synaptic cell adhesion molecules regulate various steps of synapse formation. Despite the great diversity of neuronal synapses, relatively few adhesion molecules with synaptogenic activity have been identified. Synaptic adhesion-like molecules (SALMs) are members of a family of cell adhesion molecules known to regulate neurite outgrowth and synapse maturation; however, the role of SALMs in synapse formation remains unknown. We found that expression of the SALM family proteins SALM3 and SALM5 in nonneural and neural cells induces both excitatory and inhibitory presynaptic differentiation in contacting axons. SALM3 and SALM5 proteins are enriched in synaptic fractions, and form strong (SALM3) or weak (SALM5) complexes with postsynaptic density-95 (PSD-95), an abundant postsynaptic scaffolding protein at excitatory synapses. Aggregation of SALM3, but not SALM5, on dendritic surfaces induces clustering of PSD-95. Knockdown of SALM5 reduces the number and function of excitatory and inhibitory synapses. These results suggest that selected SALM family proteins regulate synapse formation, and that SALM3 and SALM5 may promote synapse formation through distinct mechanisms.

Annotation

Gene Ontology Annotations    

Biological Process

Cellular Component

Objects Annotated

Genes (Rattus norvegicus)
Lrfn4  (leucine rich repeat and fibronectin type III domain containing 4)
Lrfn5  (leucine rich repeat and fibronectin type III domain containing 5)


Additional Information