The language of histone crosstalk - PubMed (original) (raw)

Review

The language of histone crosstalk

Jung-Shin Lee et al. Cell. 2010.

Abstract

It has been suggested that a specific pattern of histone posttranslational modifications and their crosstalk may constitute a code that determines transcriptional outcomes. However, recent studies indicate that histone modifications have context-dependent effects, making their interplay more like a language within the chromatin signaling pathway than a code.

PubMed Disclaimer

Figures

Figure 1. Examples of Histone crosstalk

(A) The first characterized example of histone crosstalk is the stimulation of acetyltransferase activity of GCN5 towards the histone H3 tail by prior phosphorylation (P) of serine 10. Acetylation, Ac. (B) Crosstalk among histone modifications can span more than one histone. Monoubiquitination of histone H2B can lead to the trimethylation of lysine 4 in the histone 3 tail (H3K4) by Set1/COMPASS. However, H3K4 methylation by COMPASS and COMPASS-like complexes can be blocked if the nearby arginine of H3 is already methylated.

Figure 2. Context dependent outcomes of histone crosstalk

(A) Zippo and colleagues (Zippo et al., 2009) uncover a new form of histone crosstalk by studying the transcriptional control of FOS1L, a gene activated in response to serum. Activation requires the binding of PIM1 to the FOS1L enhancer. PIM1 is a kinase responsible for phosphorylation (P) of serine 10 on the histone H3 tail (H3S10). Phosphorylated H3S10 creates a binding site for 14-3-3, a phosphoserine binding protein. Acetylation (Ac) of lysine 16 on the H4 (H4K16) tail occurs through interaction of 14-3-3 with the histone acetyltransferase MOF. Acetylated H4K16 can in turn form a binding site for the bromodomain-containing protein Brd4, a component of P-TEFb, a kinase that phosphorylates the C-terminal domain of RNA Pol II to facilitate transcription elongation. However, at an earlier stage of serum stimulation, an MSK1/2 kinase is recruited to the promoter where it phosphorylates H3S10. 14-3-3 is then recruited to the promoter, but unlike the situation at the enhancer, MOF is not recruited to the promoter. Thus, the timing, location, and perhaps identity of the H3 kinase, and not the H3S10 modification alone, determines downstream events. (B) Another example of how the order of implementation of histone modifications can affect transcription comes from work from Wang et al. (2009). They report that despite correlations between histone acetylation and H3K4 methylation, artificially increasing acetylation through treatment of cells with deacetylase inhibitors (HDACs) does not lead to productive transcription, despite the presence of H3K4 methylation and Pol II recruitment. Therefore, patterns of histone modifications cannot simply be “read”, but have distinct effects depending on the cellular context and upstream signaling events.

Cited by

Functional decorations: post-translational modifications and heart disease delineated by targeted proteomics.
Liddy KA, White MY, Cordwell SJ. Liddy KA, et al. Genome Med. 2013 Feb 28;5(2):20. doi: 10.1186/gm424. eCollection 2013. Genome Med. 2013. PMID: 23445784 Free PMC article. Review.
TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS.
Deplus R, Delatte B, Schwinn MK, Defrance M, Méndez J, Murphy N, Dawson MA, Volkmar M, Putmans P, Calonne E, Shih AH, Levine RL, Bernard O, Mercher T, Solary E, Urh M, Daniels DL, Fuks F. Deplus R, et al. EMBO J. 2013 Mar 6;32(5):645-55. doi: 10.1038/emboj.2012.357. Epub 2013 Jan 25. EMBO J. 2013. PMID: 23353889 Free PMC article.
Quantitative proteomic analysis of histone modifications.
Huang H, Lin S, Garcia BA, Zhao Y. Huang H, et al. Chem Rev. 2015 Mar 25;115(6):2376-418. doi: 10.1021/cr500491u. Epub 2015 Feb 17. Chem Rev. 2015. PMID: 25688442 Free PMC article. Review. No abstract available.
Tlx3 promotes glutamatergic neuronal subtype specification through direct interactions with the chromatin modifier CBP.
Shimomura A, Patel D, Wilson SM, Koehler KR, Khanna R, Hashino E. Shimomura A, et al. PLoS One. 2015 Aug 10;10(8):e0135060. doi: 10.1371/journal.pone.0135060. eCollection 2015. PLoS One. 2015. PMID: 26258652 Free PMC article.
Dual Chromatin and Cytoskeletal Remodeling by SETD2.
Park IY, Powell RT, Tripathi DN, Dere R, Ho TH, Blasius TL, Chiang YC, Davis IJ, Fahey CC, Hacker KE, Verhey KJ, Bedford MT, Jonasch E, Rathmell WK, Walker CL. Park IY, et al. Cell. 2016 Aug 11;166(4):950-962. doi: 10.1016/j.cell.2016.07.005. Cell. 2016. PMID: 27518565 Free PMC article.

References

1. Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit Composition and Substrate Specificity of a MOF-containing Histone Acetyltransferase Distinct from the Male-specific Lethal (MSL) Complex. J Biol Chem. 2010;285:4268–4272. - PMC - PubMed
1. Cheung P, Tanner KG, Cheung WL, Sassone-Corsi P, Denu JM, Allis CD. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol Cell. 2000;5:905–915. - PubMed
1. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009;325:834–840. - PubMed
1. Fischle W, Tseng BS, Dormann HL, Ueberheide BM, Garcia BA, Shabanowitz J, Hunt DF, Funabiki H, Allis CD. Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature. 2005;438:1116–1122. - PubMed
1. Guccione E, Bassi C, Casadio F, Martinato F, Cesaroni M, Schuchlautz H, Luscher B, Amati B. Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive. Nature. 2007;449:933–937. - PubMed

The language of histone crosstalk - PubMed (original) (raw)