Academic journal article Environmental Health Perspectives

Misfolded Protein Presents Potential Molecular Explanation for Autism Spectrum Disorders

Academic journal article Environmental Health Perspectives

Misfolded Protein Presents Potential Molecular Explanation for Autism Spectrum Disorders

Article excerpt

Currently, there is only very limited information available on the etiology and biological basis of the autism spectrum disorders, although a mutation in the neuroligin 3 gene has caught researchers' attention in recent studies. Now NIEHS grantees Mark H. Ellisman and Palmer Taylor at the University of California, San Diego, and their colleagues have determined that homologous mutations in the genes coding the proteins butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) cause defects in protein expression similar to those seen with neuroligin 3, shedding further light on a potential molecular mechanism underlying autism.

The neuroligins, BChE, and AChE are members of the [alpha],[beta]-hydrolase fold family of proteins. The neuroligin 3 mutation, an arginine-to-cysteine substitution, was identified in a set of twins and has been shown to result in most of the expressed protein being retained within the endoplasmic reticulum. The small amount of protein that does reach the surface of the cell shows little binding affinity for its partner, [beta]-neurexin, suggesting possible misfolding of the protein. …

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