Bioinformatics analysis of proteins interacting with different actin isoforms.

Abstract

Actin is one of the most widespread and most conserved proteins. At the same time, six actin isoforms are known, encoded by different genes. These isoforms differ slightly in amino acid sequence and have similar structures, but differ in localization and functioning. During functioning, actin interacts with a large number of proteins, which are combined according to this feature into a pool of so-called actin-binding proteins. The question arises whether and how the proteins interacting with different actin isoforms differ. Since the pool of actin-binding proteins includes hundreds of proteins, it was logical to use bioinformatics analysis to solve the questions. In this work, it is shown that the functionality of the α-, β-, and γ-actin interactomes differ significantly, but their structural characteristics are close.