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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Leucine rich repeat and fibronectin type III domain containing 3

Top mentioned proteins: fibronectin, PSD-95, SAP97, NMDA receptor, NR2A
Papers on SALM4
The SALM/Lrfn family of leucine-rich repeat-containing cell adhesion molecules.
Kim et al., Taej┼Ćn, South Korea. In Semin Cell Dev Biol, 2011
SALMs 1-3 contain a C-terminal PDZ-binding motif, which interacts with PSD-95, an abundant postsynaptic scaffolding protein, whereas SALM4 and SALM5 lack PDZ binding.
Flotillin-1 mediates neurite branching induced by synaptic adhesion-like molecule 4 in hippocampal neurons.
Wenthold et al., Bethesda, United States. In Mol Cell Neurosci, 2010
Here we establish flotillin-1 (flot-1) as a molecular mediator of neurite branching for SALM4.
Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.
Wenthold et al., Bethesda, United States. In Mol Cell Neurosci, 2008
Data show that the C-terminal PDZ binding domains of synaptic adhesion-like molecules (SALMs)1-3 are required for neurite outgrowth, and that the N-termini of SALMs 2 and 4 are alsoinvolved in neurite outgrowth.
The SALM family of adhesion-like molecules forms heteromeric and homomeric complexes.
Wenthold et al., Bethesda, United States. In J Biol Chem, 2008
The ability of SALM4 to form trans interactions is due to its extracellular N terminus because chimeras of SALM4 N terminus and SALM2 C terminus can form trans interactions, whereas chimeras of SALM2 N terminus and SALM4 C terminus cannot.
A conserved gene family encodes transmembrane proteins with fibronectin, immunoglobulin and leucine-rich repeat domains (FIGLER).
Cooper et al., Birmingham, United States. In Bmc Biol, 2006
RESULTS: Our database search identified a family of nine gene candidates, which we have provisionally named fibronectin immunoglobulin leucine-rich repeat (FIGLER).
Comparative analysis of structure, expression and PSD95-binding capacity of Lrfn, a novel family of neuronal transmembrane proteins.
Aruga et al., Wako, Japan. In Gene, 2006
Leucine-rich repeat and fibronectin III domain-containing (Lrfn) has five members in mouse and human (Lrfn1, Lrfn2, Lrfn3, Lrfn4, Lrfn5), and homologues in other vertebrates.
A novel family of adhesion-like molecules that interacts with the NMDA receptor.
Wenthold et al., Bethesda, United States. In J Neurosci, 2006
The family members, SALM1-SALM4, have a single transmembrane (TM) domain and contain extracellular leucine-rich repeats, an Ig C2 type domain, a fibronectin type III domain, and an intracellular postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1 (PDZ) binding domain, which is present on all members except SALM4.
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