Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

The palmitoyl acyltransferase HIP14 shares a high proportion of interactors with huntingtin: implications for a role in the pathogenesis of Huntington's disease.

Butland SL, Sanders SS, Schmidt ME, Riechers SP, Lin DT, Martin DD, Vaid K, Graham RK, Singaraja RR, Wanker EE, Conibear E, Hayden MR

HIP14 is the most highly conserved of 23 human palmitoyl acyltransferases (PATs) that catalyze the post-translational addition of palmitate to proteins, including huntingtin (HTT). HIP14 is dysfunctional in the presence of mutant HTT (mHTT), the causative gene for Huntington disease (HD), and we hypothesize that reduced palmitoylation of HTT and other HIP14 substrates contributes to the pathogenesis of the disease. ... [more]

Hum. Mol. Genet. Aug. 01, 2014; 23(15);4142-60 [Pubmed: 24705354]

Throughput

  • High Throughput

Curated By

  • BioGRID