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假激酶在细胞信号转导中的功能.

Authors :
伍 铤
王 韵
Source :
Chinese Journal of Biochemistry & Molecular Biology. Oct2023, Vol. 39 Issue 10, p1401-1407. 7p.
Publication Year :
2023

Abstract

Protein kinases regulate signaling pathways in eukaryotic cells. The phosphorylation function of kinases has attracted the attention of scientists and been deeply studied. However, some kinases are called “pseudokinases” due to missing of the key amino acids in the key motif during evolution, which leads to disruption of their phosphoryl-transfer activity. The fact that these pseudokinases are conserved across species argues that although pseudokinases have lost their phosphoryl-transfer activity, they may acquire the phosphorylation-independent functions and participate in the cellular signal transduction as well. The phosphorylation-independent functions of pseudokinases are listed as follows: 1. Directly regulating the phosphorylation activity of active kinases by binding with them; 2. Regulating the phosphorylation activity of active kinases by competitive inhibition; 3. Acting as molecular switches to perform key non-catalytic functions; 4. Acting as signaling scaffolds to assist in cell signaling; 5. Exerting catalytic functions other than phosphorylation activity. These functions have been shown to be involved in important physiological processes such as development, immunity and metabolism. Mutations or abnormal expression of pseudokinases are associated with the occurrence of various diseases such as tumors, neurological diseases, metabolic diseases and autoimmune diseases. In this article, we summarize the functions of pseudokinases in cellular signal transduction and provide a perspective for the future directions in the study of pseudokinases. [ABSTRACT FROM AUTHOR]

Details

Language :
Chinese
ISSN :
10077626
Volume :
39
Issue :
10
Database :
Academic Search Index
Journal :
Chinese Journal of Biochemistry & Molecular Biology
Publication Type :
Academic Journal
Accession number :
174190306
Full Text :
https://doi.org/10.13865/j.cnki.cjbmb.2023.02.1511