Journal
LIFE-BASEL
Volume 11, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/life11090957
Keywords
protein phosphorylation; protein kinase; protein phosphatase; SLiMs; substrate recognition; structural regulation; protein structure
Categories
Funding
- Jeju National University
Ask authors/readers for more resources
Protein phosphorylation, a crucial post-translational modification process, is regulated by protein kinases and protein phosphatases. These reversible enzyme activities provide a regulatory mechanism for diverse protein functions in cellular processes.
Protein phosphorylation is one of the most widely observed and important post-translational modification (PTM) processes. Protein phosphorylation is regulated by protein kinases, each of which covalently attaches a phosphate group to an amino acid side chain on a serine (Ser), threonine (Thr), or tyrosine (Tyr) residue of a protein, and by protein phosphatases, each of which, conversely, removes a phosphate group from a phosphoprotein. These reversible enzyme activities provide a regulatory mechanism by activating or deactivating many diverse functions of proteins in various cellular processes. In this review, their structures and substrate recognition are described and summarized, focusing on Ser/Thr protein kinases and protein Ser/Thr phosphatases, and the regulation of protein structures by phosphorylation. The studies reviewed here and the resulting information could contribute to further structural, biochemical, and combined studies on the mechanisms of protein phosphorylation and to drug discovery approaches targeting protein kinases or protein phosphatases.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available