Neuroligins 3 and 4X interact with syntrophin-gamma2, and the interactions are affected by autism-related mutations

Hidekuni Yamakawa; Satoko Oyama; Hiroaki Mitsuhashi; Noboru Sasagawa; Shigeo Uchino; Shinichi Kohsaka; Shoichi Ishiura

doi:10.1016/j.bbrc.2007.01.127

Neuroligins 3 and 4X interact with syntrophin-gamma2, and the interactions are affected by autism-related mutations

Biochem Biophys Res Commun. 2007 Mar 30;355(1):41-6. doi: 10.1016/j.bbrc.2007.01.127. Epub 2007 Jan 31.

Authors

Hidekuni Yamakawa¹, Satoko Oyama, Hiroaki Mitsuhashi, Noboru Sasagawa, Shigeo Uchino, Shinichi Kohsaka, Shoichi Ishiura

Affiliation

¹ Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo, 3-8-1 Komaba, Meguro-ku 153-8902, Japan.

PMID: 17292328
DOI: 10.1016/j.bbrc.2007.01.127

Abstract

Recently, neuroligins (NLs)3 and 4X have received much attention as autism-related genes. Here, we identified syntrophin-gamma2 (SNTG2) as a de novo binding partner of NL3. SNTG2 also bound to NL4X and NL4Y. Interestingly, the binding was influenced by autism-related mutations, implying that the impaired interaction between NLs and SNTG2 contributes to the etiology of autism.

MeSH terms

Autistic Disorder / genetics*
Autistic Disorder / pathology
Carrier Proteins / genetics
Carrier Proteins / metabolism*
Cell Adhesion Molecules, Neuronal
Cloning, Molecular
Humans
Membrane Proteins / genetics
Membrane Proteins / metabolism*
Muscle Proteins / genetics
Muscle Proteins / metabolism*
Mutation*
Nerve Tissue Proteins / genetics
Nerve Tissue Proteins / metabolism*
Recombinant Fusion Proteins / metabolism
Recombinant Proteins / metabolism
Restriction Mapping
Saccharomyces cerevisiae / genetics
Synapses / pathology
gamma-Aminobutyric Acid / physiology

Substances

Carrier Proteins
Cell Adhesion Molecules, Neuronal
Membrane Proteins
Muscle Proteins
NLGN4X protein, human
Nerve Tissue Proteins
Recombinant Fusion Proteins
Recombinant Proteins
SNTG2 protein, human
neuroligin 3
gamma-Aminobutyric Acid