Histone acetyltransferase KAT8

Definition:

Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex. Can also acetylate TP53/p53 at 'Lys-120'.

References:

[1]. Arun Gupta, et al. Involvement of human MOF in ATM function. Mol Cell Biol. 2005 Jun;25(12):5292-305. [Content Brief]

[2]. Hua Yuan, et al. MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J. 2012 Jan 4;31(1):58-70. [Content Brief]

[3]. Jan Kadlec, et al. Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. Nat Struct Mol Biol. 2011 Feb;18(2):142-9. [Content Brief]

[4]. Lin Li, et al. Lysine acetyltransferase 8 is involved in cerebral development and syndromic intellectual disability. J Clin Invest. 2020 Mar 2;130(3):1431-1445. [Content Brief]

[5]. Sascha Mendjan, et al. Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila. Mol Cell. 2006 Mar 17;21(6):811-23. [Content Brief]

[6]. Jing Huang, et al. Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex. Cell Res. 2012 Jun;22(6):1078-81. [Content Brief]

[7]. Patricia S Pardo, et al. MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation. J Biol Chem. 2002 Dec 27;277(52):50860-6. [Content Brief]

[8]. Edwin R Smith, et al. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol. 2005 Nov;25(21):9175-88. [Content Brief]

[9]. Yong Cai, et al. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. [Content Brief]

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