Huntingtin-associated protein 1 (HAP1) is a neural interactor of huntingtin in Huntington's disease and interacts with gene products in a number of other neurodegenerative diseases.
Huntingtin-associated protein 1 (HAP1) is a neuronal interactor with causatively polyglutamine (polyQ)-expanded huntingtin in Huntington's disease and also associated with pathologically polyQ-expanded androgen receptor (AR) in spinobulbar muscular atrophy (SBMA), being considered as a protective factor against neurodegenerative apoptosis.
In this study, we investigated the expression of huntingtin-associated protein 1 (HAP1), the ligand of HD's production, in breast tumor and normal tissues.
Kalirin is a protein crucially involved in spine plasticity and its interaction with huntingtin-associated protein-1 (HAP-1) and a potential protein dysfunction might contribute to spine pathogenesis in HD.
In previous candidate gene studies, associations of the age at onset (AO) in Huntington disease (HD) have been reported with genetic variations in the genes encoding adenosinergic A(2A) receptor (ADORA2A), human huntingtin-associated protein-1 (HAP1) and the single base excision repair enzyme, 7,8-dihydro-8-oxoguanine-DNA glycosylase (OGG1).
The selective neuropathology in HD is thought to be mediated in part through interactions with other proteins including the Huntington Associated Protein, HAP-1, which is predominantly expressed in the brain.
We have used the yeast two hybrid system to demonstrate that htt amino acids 171-230 are necessary for the hap1-htt binding and that hapl does not interact with the transgene exon 1 protein in a transgenic model of HD.
HAP1, a protein that interacts with huntingtin (Huntington's disease protein), has an expression profile that intriguingly mirrors the selective neurodegeneration seen in Huntington's disease.
The possible relationship of HAP1 and nNOS in the brain is reminiscent of the relationship of dystrophin and nNOS in skeletal muscle and suggests a role of NO in Huntington disease, analogous to its postulated role in Duchenne muscular dystrophy.