AN INTERACTION OF PROTEINS OF THE 14-3-3 FAMILY WITH CYTOSKELETAL SYSTEM

Abstract

Phosphorylation of serine, threonine, and tyrosine residues catalyzed by protein kinases is one of the widespread types of posttranslational modifications that affect the structure and properties of a protein. The transfer of the phosphoric acid residue is accompanied by a change in charge, which often leads to significant conformational rearrangements that affect the structure, properties, and functional activity of phosphorylated proteins. There are several families of proteins in the cell that recognize and specifically interact with certain regions of phosphorylated proteins. One of these families is represented by proteins 14-3-3, which were discovered more than 40 years ago during the systematic classification of nerve tissue proteins, where their content exceeds 1% of the proteome [1, 2]. To date, more than 300 different target proteins capable of interacting with 14-3-3 have been described [3]. Representatives of the 14-3-3 family are practically ubiquitous and act as regulators of apoptosis, cell cycle, division, transcription, replication, functioning of ion channels and transporters, and cytoskeleton organization. In addition, the number of reports on the involvement of 14-3-3 in the development of a number of neurodegenerative and oncological diseases has increased recently. All this aroused an increased interest in the proteins of this family. This review is devoted to the description of the structure, properties, and mechanisms of regulation of the activity of proteins of the 14-3-3 family, as well as the analysis of their interaction with substrate proteins and their possible participation in the regulation of the cytoskeleton.