Language
English
Publication Date
8-1-2022
Journal
Molecular Aspects of Medicine
DOI
10.1016/j.mam.2022.101097
PMID
35400524
PMCID
PMC9378605
PubMedCentral® Posted Date
8-1-2023
PubMedCentral® Full Text Version
Author MSS
Abstract
Protein post-translational modifications (PTMs) profoundly influence protein functions and play crucial roles in essentially all cell biological processes. The diverse realm of PTMs and their crosstalk is linked to many critical signaling events involved in neoplastic transformation, carcinogenesis and metastasis. The pathological roles of various PTMs are implicated in all aspects of cancer hallmark functions, cancer metabolism and regulation of tumor microenvironment. Study of PTMs has become an important area in cancer research to understand cancer biology and discover novel biomarkers and therapeutic targets. With a limited scope, this review attempts to discuss some PTMs of high frequency with recognized importance in cancer biology, including phosphorylation, acetylation, glycosylation, palmitoylation and ubiquitination, as well as their implications in clinical applications. These protein modifications are among the most abundant PTMs and profoundly implicated in carcinogenesis.
Keywords
Acetylation, Carcinogenesis, Humans, Neoplasms, Phosphorylation, Protein Processing, Post-Translational, Proteins, Tumor Microenvironment, post-translational modifications, cancer, tumorigenesis, pathological role, signaling pathways, proteomics
Published Open-Access
yes
Recommended Citation
, "Pathological Implication of Protein Post-translational Modifications in Cancer" (2022). Faculty, Staff and Students Publications. 1340.
https://digitalcommons.library.tmc.edu/baylor_docs/1340