Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.

doi:10.1038/nature11922

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Article

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS.

Nature - 28 Mar 2013

Kim Hong Joo, Kim Nam Chul, Wang Yong-Dong, Scarborough Emily A, Moore Jennifer, Diaz Zamia, MacLea Kyle S, Freibaum Brian, Li Songqing, Molliex Amandine, Kanagaraj Anderson P, Carter Robert, Boylan Kevin B, Wojtas Aleksandra M, Rademakers Rosa, Pinkus Jack L, Greenberg Steven A, Trojanowski John Q, Traynor Bryan J, Smith Bradley N, Topp Simon, Gkazi Athina-Soragia, Miller Jack, Shaw Christopher E, Kottlors Michael, Kirschner Janbernd, Pestronk Alan, Li Yun R, Ford Alice Flynn, Gitler Aaron D, Benatar Michael, King Oliver D, Kimonis Virginia E, Ross Eric D, Weihl Conrad C, Shorter James, Taylor J Paul

Abstract excerpt

Algorithms designed to identify canonical yeast prions predict that around 250 human proteins, including several RNA-binding proteins associated with neurodegenerative disease, harbour a distinctive prion-like domain (PrLD) enriched in uncharged polar amino acids and glycine. PrLDs in RNA-binding proteins are essential for the assembly of ribonucleoprotein granules. However, the interplay between human PrLD...

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PMID: 23455423
DOI: 10.1038/nature11922
PMCID: PMC3756911

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