WDR5, a complexed protein

Raymond C. Trievel; Ali Shilatifard

doi:10.1038/nsmb0709-678

WDR5, a complexed protein

Raymond C. Trievel, Ali Shilatifard

Biochemistry and Molecular Genetics

Research output: Contribution to journal › Comment/debate › peer-review

108 Scopus citations

Abstract

The WD40 protein WDR5 is a core subunit of the human MLL and SET1 (hCOMPASS) histone H3 Lys4 (H3K4) methyltransferase complexes. Although initial studies suggested that WDR5 interacts with methylated H3K4 to catalyze Lys4 trimethylation, recent work has revealed that it binds an arginine-bearing motif in MLL1, promoting complex assembly and activity. These findings suggest that WDR5 functions as a peptidyl arginine recognition factor that facilitates the assembly of hCOMPASS and other chromatin-modifying complexes.

Original language	English (US)
Pages (from-to)	678-680
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	16
Issue number	7
DOIs	https://doi.org/10.1038/nsmb0709-678
State	Published - Jul 2009

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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title = "WDR5, a complexed protein",

abstract = "The WD40 protein WDR5 is a core subunit of the human MLL and SET1 (hCOMPASS) histone H3 Lys4 (H3K4) methyltransferase complexes. Although initial studies suggested that WDR5 interacts with methylated H3K4 to catalyze Lys4 trimethylation, recent work has revealed that it binds an arginine-bearing motif in MLL1, promoting complex assembly and activity. These findings suggest that WDR5 functions as a peptidyl arginine recognition factor that facilitates the assembly of hCOMPASS and other chromatin-modifying complexes.",

author = "Trievel, {Raymond C.} and Ali Shilatifard",

note = "Funding Information: We thank D. Bochar, J. Workman and E. Smith for reading the manuscript and providing insightful comments, and L. Shilatifard for editorial assistance. This work was supported by grants from the US National Institute of General Medical Sciences (NIGMS; 5R01GM073839) to R.C.T. and the US National Cancer Institute (NCI; 5R01CA089455) to A.S.H.",

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AU - Shilatifard, Ali

N1 - Funding Information: We thank D. Bochar, J. Workman and E. Smith for reading the manuscript and providing insightful comments, and L. Shilatifard for editorial assistance. This work was supported by grants from the US National Institute of General Medical Sciences (NIGMS; 5R01GM073839) to R.C.T. and the US National Cancer Institute (NCI; 5R01CA089455) to A.S.H.

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N2 - The WD40 protein WDR5 is a core subunit of the human MLL and SET1 (hCOMPASS) histone H3 Lys4 (H3K4) methyltransferase complexes. Although initial studies suggested that WDR5 interacts with methylated H3K4 to catalyze Lys4 trimethylation, recent work has revealed that it binds an arginine-bearing motif in MLL1, promoting complex assembly and activity. These findings suggest that WDR5 functions as a peptidyl arginine recognition factor that facilitates the assembly of hCOMPASS and other chromatin-modifying complexes.

AB - The WD40 protein WDR5 is a core subunit of the human MLL and SET1 (hCOMPASS) histone H3 Lys4 (H3K4) methyltransferase complexes. Although initial studies suggested that WDR5 interacts with methylated H3K4 to catalyze Lys4 trimethylation, recent work has revealed that it binds an arginine-bearing motif in MLL1, promoting complex assembly and activity. These findings suggest that WDR5 functions as a peptidyl arginine recognition factor that facilitates the assembly of hCOMPASS and other chromatin-modifying complexes.

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WDR5, a complexed protein

Abstract

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