» Articles » PMID: 34059135

Emerging Roles of Non-histone Protein Crotonylation in Biomedicine

Overview
Journal Cell Biosci
Publisher Biomed Central
Specialty Biology
Date 2021 Jun 1
PMID 34059135
Citations 15
Authors
Affiliations
Soon will be listed here.
Abstract

Crotonylation of proteins is a newly found type of post-translational modifications (PTMs) which occurs leadingly on the lysine residue, namely, lysine crotonylation (Kcr). Kcr is conserved and is regulated by a series of enzymes and co-enzymes including lysine crotonyltransferase (writer), lysine decrotonylase (eraser), certain YEATS proteins (reader), and crotonyl-coenzyme A (donor). Histone Kcr has been substantially studied since 2011, but the Kcr of non-histone proteins is just an emerging field since its finding in 2017. Recent advances in the identification and quantification of non-histone protein Kcr by mass spectrometry have increased our understanding of Kcr. In this review, we summarized the main proteomic characteristics of non-histone protein Kcr and discussed its biological functions, including gene transcription, DNA damage response, enzymes regulation, metabolic pathways, cell cycle, and localization of heterochromatin in cells. We further proposed the performance of non-histone protein Kcr in diseases and the prospect of Kcr manipulators as potential therapeutic candidates in the diseases.

Citing Articles

Metabolism-driven chromatin dynamics: Molecular principles and technological advances.

Sahu V, Lu C Mol Cell. 2025; 85(2):262-275.

PMID: 39824167 PMC: 11750176. DOI: 10.1016/j.molcel.2024.12.012.


Regulatory Mechanism of Protein Crotonylation and Its Relationship with Cancer.

Yang S, Fan X, Yu W Cells. 2024; 13(21.

PMID: 39513918 PMC: 11545499. DOI: 10.3390/cells13211812.


PTBP1 crotonylation promotes colorectal cancer progression through alternative splicing-mediated upregulation of the PKM2 gene.

Hou J, Wang X, Chang H, Wang X, Hao S, Gao Y J Transl Med. 2024; 22(1):995.

PMID: 39497094 PMC: 11536555. DOI: 10.1186/s12967-024-05793-5.


Protein lysine crotonylation in cellular processions and disease associations.

Zhao H, Han Y, Zhou P, Guan H, Gao S Genes Dis. 2024; 11(5):101060.

PMID: 38957707 PMC: 11217610. DOI: 10.1016/j.gendis.2023.06.029.


p53 deficiency mediates cisplatin resistance by upregulating RRM2 and crotonylation of RRM2 through the downregulation of SIRT7.

Sun L, Li Y, Wang M, Luo L, Sun R, Chen Y Front Mol Biosci. 2024; 11:1423594.

PMID: 38894712 PMC: 11183501. DOI: 10.3389/fmolb.2024.1423594.


References
1.
Lin H, Su X, He B . Protein lysine acylation and cysteine succination by intermediates of energy metabolism. ACS Chem Biol. 2012; 7(6):947-60. PMC: 3376250. DOI: 10.1021/cb3001793. View

2.
Reed S, Hagen J, Tompkins V, Thies K, Quelle F, Quelle D . Nuclear interactor of ARF and Mdm2 regulates multiple pathways to activate p53. Cell Cycle. 2014; 13(8):1288-98. PMC: 4049965. DOI: 10.4161/cc.28202. View

3.
Sun J, Qiu C, Qian W, Wang Y, Sun L, Li Y . Ammonium triggered the response mechanism of lysine crotonylome in tea plants. BMC Genomics. 2019; 20(1):340. PMC: 6501322. DOI: 10.1186/s12864-019-5716-z. View

4.
Wisniewski J, Zougman A, Mann M . Nepsilon-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function. Nucleic Acids Res. 2007; 36(2):570-7. PMC: 2241850. DOI: 10.1093/nar/gkm1057. View

5.
Wan J, Liu H, Chu J, Zhang H . Functions and mechanisms of lysine crotonylation. J Cell Mol Med. 2019; 23(11):7163-7169. PMC: 6815811. DOI: 10.1111/jcmm.14650. View