ArticleScientific reports2016
Pits, a protein interacting with Ttk69 and Sin3A, has links to histone deacetylation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Loss of IRF2BPL impairs neuronal maintenance through excess Wnt signaling.Science advances · 2022Article
- Pits and CtBP Control Tissue Growth inGenetics · 2020Article
- Inactive Tlk associating with Tak1 increases p38 MAPK activity to prolong the G2 phase.Scientific reports · 2019Article
- IRF2BPL Is Associated with Neurological Phenotypes.American journal of human genetics · 2018Article
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1 author at 1 institution in 1 country.
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Abstract
Histone deacetylation plays an important role in transcriptional repression. Previous results showed that the genetic interaction between ttk and rpd3, which encodes a class I histone deacetylase, is required for tll repression. This study investigated the molecular mechanism by which Ttk69 recruits Rpd3. Using yeast two-hybrid screening and datamining, one novel protein was found that weakly interacts with Ttk69 and Sin3A, designated as Protein interacting with Ttk69 and Sin3A (Pits). Pits protein expressed in the early stages of embryos and bound to the region of the tor response element in vivo. Expanded tll expression patterns were observed in embryos lacking maternal pits activity and the expansion was not widened by reducing either maternal ttk or sin3A activity. However, in embryos with simultaneously reduced maternal pits and sin3A activities or maternal pits, sin3A and ttk activities, the proportions of the embryos with expanded tll expression were significantly increased. These results indicate that all three gene activities are involved in tll repression. Level of histone H3 acetylation in the tll proximal region was found to be elevated in embryo with reduced these three gene activities. In conclusion, Ttk69 causes the histone deacetylation-mediated repression of tll via the interaction of Pits and Sin3A.
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