ArticleJournal of neurochemistry2011
Dimerization of the DYT6 dystonia protein, THAP1, requires residues within the coiled-coil domain.
Article in Journal of neurochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Transcriptional regulatory network for neuron-glia interactions and its implication for DYT6 dystonia.Dystonia (Lausanne, Switzerland) · 2023Article
- Pan-Cancer Analysis Reveals the Prognostic Potential of the THAP9/THAP9-AS1 Sense-Antisense Gene Pair in Human Cancers.Non-coding RNA · 2022Article
- A pathogenic DYT-THAP1 dystonia mutation causes hypomyelination and loss of YY1 binding.Human molecular genetics · 2022Article
- Dystonia-specific mutations in THAP1 alter transcription of genes associated with neurodevelopment and myelin.American journal of human genetics · 2021Article
- Emerging and converging molecular mechanisms in dystonia.Journal of neural transmission (Vienna, Austria : 1996) · 2021Review
- Isolated dystonia: clinical and genetic updates.Journal of neural transmission (Vienna, Austria : 1996) · 2021Review
- Article
- THAP1: Role in Mouse Embryonic Stem Cell Survival and Differentiation.Stem cell reports · 2017Article
- The DYT6 Dystonia Protein THAP1 Regulates Myelination within the Oligodendrocyte Lineage.Developmental cell · 2017Article
- In-depth Characterization of the Homodimerization Domain of the Transcription Factor THAP1 and Dystonia-Causing Mutations Therein.Journal of molecular neuroscience : MN · 2017Article
- Abnormalities of motor function, transcription and cerebellar structure in mouse models of THAP1 dystonia.Human molecular genetics · 2015Article
- Inherited isolated dystonia: clinical genetics and gene function.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2014Review
- Dystonia type 6 gene product Thap1: identification of a 50 kDa DNA-binding species in neuronal nuclear fractions.Acta neuropathologica communications · 2014Article
- A rare sequence variant in intron 1 of THAP1 is associated with primary dystonia.Molecular genetics & genomic medicine · 2014Article
- NMR studies of a new family of DNA binding proteins: the THAP proteins.Journal of biomolecular NMR · 2013Review
- Mutation screening of the DYT6/THAP1 gene in Serbian patients with primary dystonia.Journal of neurology · 2013Article
- Article
- Genotype-phenotype correlations in THAP1 dystonia: molecular foundations and description of new cases.Parkinsonism & related disorders · 2012Review
- The genetics of dystonias.Advances in genetics · 2012Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Thanatos-associated [THAP] domain-containing apoptosis-associated protein 1 (THAP1) is a DNA-binding protein that has been recently associated with DYT6 dystonia, a hereditary movement disorder involving sustained, involuntary muscle contractions. A large number of dystonia-related mutations have been identified in THAP1 in diverse patient populations worldwide. Previous reports have suggested that THAP1 oligomerizes with itself via a C-terminal coiled-coil domain, raising the possibility that DYT6 mutations in this region might affect this interaction. In this study, we examined the ability of wild-type THAP1 to bind itself and the effects on this interaction of the following disease mutations: C54Y, F81L, ΔF132, T142A, I149T, Q154fs180X, and A166T. The results confirmed that wild-type THAP1 associated with itself and most of the DYT6 mutants tested, except for the Q154fs180X variant, which loses most of the coiled-coil domain because of a frameshift at position 154. However, deletion of C-terminal residues after position 166 produced a truncated variant of THAP1 that was able to bind the wild-type protein. The interaction of THAP1 with itself therefore required residues within a 13-amino acid region (aa 154-166) of the coiled-coil domain. Further inspection of this sequence revealed elements highly consistent with previous descriptions of leucine zippers, which serve as dimerization domains in other transcription factor families. Based on this similarity, a structural model was generated to predict how hydrophobic residues in this region may mediate dimerization. These observations offer additional insight into the role of the coiled-coil domain in THAP1, which may facilitate future analyses of DYT6 mutations in this region.
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