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Evaluation of post-translational modifications in histone proteins: A review on histone modification defects in developmental and neurological disorders

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Abstract

Post-translational modification (PTM) in histone proteins is a covalent modification which mainly consists of methylation, phosphorylation, acetylation, ubiquitylation, SUMOylation, glycosylation, and ADP-ribosylation. PTMs have fundamental roles in chromatin structure and function. Histone modifications have also been known as epigenetic markers. The PTMs that have taken place in histone proteins can affect gene expression by altering chromatin structure. Histone modifications act in varied biological processes such as transcriptional activation/inactivation, chromosome packaging, mitosis, meiosis, apoptosis, and DNA damage/repair. Defects in the PTMs pathway have been associated with the occurrence and progression of various human diseases, such as cancer, heart failure, autoimmune diseases, and neurodegenerative disorders such as Parkinson’s disease, Alzheimer’s disease, and Huntington’s disease. Histone modifications are reversible and used as potential targets for cancer therapy and prevention. Recent different histone PTMs have key roles in cancer cells since it has been shown that histone PTMs markers in cancers are acetylation, methylation, phosphorylation, and ubiquitylation. In this review, we have summarized the six most studied histone modifications and have examined the role of these modifications in the development of cancer.

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Abbreviations

ADP:

adenosine diphosphate

ADP-ribose:

adenosine diphosphate ribose

ART:

ADP-ribosyltransferases

ARTD1/ PARP1:

poly [ADP-ribose] polymerase 1

ATM/ATR:

ATM/ATR serine/threonine kinase

ATP:

adenosine triphosphate

BRCA1:

breast cancer type 1 susceptibility protein

CARM1:

coactivator-associated arginine methyltransferase 1

ChIP:

combines chromatin immunoprecipitation

ChIP-seq:

ChIP-sequencing

CRC:

colorectal cancer

DMFS:

distant metastasis-free survival

DNase I:

deoxyribonuclease I

DSBs:

DNA double-strand breaks

E1:

ubiquitin/sumo activating

E2:

ubiquitin/sumo conjugating

E3:

ubiquitin/sumo ligase

EZH2:

Zeste homolog 2

HATs:

histone acetyltransferases

HDAC:

histone deacetylase

HMTs:

histone methyltransferases

HP1:

heterochromatin protein

LSD1:

lysine-specific histone demethyla1

MAP kinase:

mitogen-activated protein kinase

MARTs:

mono-ADP-ribosyltransferases

MLL gene fusion:

MOZ/MORF (MYST family) gene fusion

NAD:

nicotinamide adenine dinucleotide

NATs:

N-terminal acetyltransferases

OS:

overall survival

PAR:

polymeric ADP-ribose

PARP:

poly-ADP ribose synthetase

PcG proteins:

polycomb group (PcG) proteins

PO4:

phosphate

PRC2:

polycomb repressive complex 2

PRMTs:

protein arginine methyltransferases

PTMs:

post-translational modifications

RING:

really interesting new gene

RNF20:

ring finger protein 20

SET domain:

Su(var)3-9, enhancer-of-Zeste and Trithorax (suppressor of variegation, Enhancer of Zeste, and Trithorax)

SUMO:

small ubiquitin related modifier

TSSs:

transcription start sites

USP22:

ubiquitin-specific peptidase 22

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  1. Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, Jalal Ale Ahmad Highway, P.O. Box: 14115-111, Tehran, Iran

    Shahin Ramazi & Abdollah Allahverdi

  2. Bioinformatics and Computational Omics Lab (BioCOOL), Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, Jalal Ale Ahmad Highway, P.O. Box: 14115-111, Tehran, Iran

    Javad Zahiri

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Ramazi, S., Allahverdi, A. & Zahiri, J. Evaluation of post-translational modifications in histone proteins: A review on histone modification defects in developmental and neurological disorders. J Biosci 45, 135 (2020). https://doi.org/10.1007/s12038-020-00099-2

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