WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development.

By J. Wysocka, T. Swigut, T. Milne, Y. Dou, Xin Zhang, Alma Burlingame, R. Roeder, Ali H. Brivanlou, C. D. Allis. Cell, 2005

877 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/67a1ba026b32cc565f38f10ca32ef47f5203b2ba

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Citations in the corpus

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers (2007, background): “Initial biochemical studies suggested that WDR5 preferentially binds H3K4me2-containing peptides and nucleosome”
Regulation of MLL1 H3K4 methyltransferase activity by its core components (2006, background): “Although there have been reports on the functions of the individual conserved component”
Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification (2011, background): “Second, histone PTMs regulate chromatin structure and function by recruiting PTM-specific binding proteins, which recognize modified histones via specialized structural folds such as bromo-, chromo- andPHDdomains (Wysocka et al., 2005, 2006; Zeng and Zhou, 2002).”
The diverse functions of histone lysine methylation (2005, background): “Although the exact underlying mechanism is unclear, it has been proposed that the recruitment of the MLL methyl-transferase complex to dimethyl-H3-K4 as a result of WDR5 binding might convert dimethyl-H3-K4 to the trimethyl state 23 .”
The role of chromatin during transcription. (2007, background): “This phenomenon resembles how the MLL/WRD5 complex controls H3K4 methylation in humans, where histones can be mono- and dimethylated at H3K4 without WDR5, a WD-40 domain-containing protein (Wysocka et al., 2005).”
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes (2009, background): “To test this hypothesis directly, we knocked down WDR5, which is an essential subunit of the MLL complexes that are responsible for H3K4me2 and H3K4me3 modifications (Wysocka et al., 2005).”
Reading protein modifications with interaction domains (2006, background): “For example, the WD40-repeat domain of WDR5 (WD-repeat protein-5) ? a common subunit of histone H3 Lys4 methyltransferase ? preferentially binds to dimethylated Lys4 in histone H3 (Ref”
A bivalent chromatin structure marks key developmental genes in embryonic stem cells. (2006, background): “Lys4 methylation positively regulates transcription by recruiting nucleosome remodeling enzymes and histone acetylases (Santos-Rosa et al., 2003; PrayGrant et al., 2005; Sims et al., 2005; Wysocka et al., 2005), while Lys27 methylation negatively regulates transcription by promoting a compact chroma”