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Talin: Structural and Functional Relationships

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Abstract

Interaction of the extracellular matrix (ECM) with the cell cytoskeleton is realized via integrin receptors. Adhesion structures formed in the cell after the ECM binding with integrins recruit talin molecules. They are involved both in the regulation of the activity of integrin receptors and binding of these receptors with the actin cytoskeleton. Talin is an adapter protein that contains the head domain, which is an atypical FERM domain, and rod domain, consisting of coiled bundles constructed of four or five α-helices. The pattern of α-helices packing in bundles determines their resistance to tensile forces and their ability to stretch. This review focuses on identifying the relationship between the structural organization of talin and distribution of functions between the head and rod domains. The spatial orientation of subdomains (F0, F1, F2, F3) in the head domain provides accessibility of binding sites in these subdomains for effector molecules and rapid transformation of the domain itself upon talin activation. The linear arrangement of helical bundles (R1–R13) in the rod domain with a predominance of four helical bundles at the N-end of the domain and five helical bundles at its C-end determines: 1) effective interbundle interaction during the formation of an inactive (autoinhibited) form of the talin dimer and 2) the possibility of modifying individual bundle spiralization under the action of physical stimuli. As a result, binding sites with various proteins burried in helical bundles of the talin rod domain are revealed. This means that the N-terminal site of the talin molecule (head domain) transforms some biochemical signals into others. The C-terminal part of the molecule (rod domain) converts physical stimuli into biochemical or physiological signals that regulate the cellular response. The review also considers the interaction of talin with various compounds at the molecular level.

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Funding

This work was carried out within the framework of a state order to the Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, state registration no. АААА-А18-118012290371-3.

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  1. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, 194223, St. Petersburg, Russia

    V. P. Ivanova

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  1. V. P. Ivanova
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Correspondence to V. P. Ivanova.

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The author did not conduct experiments with animals or human beings.

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Translated by I. Fridlyanskaya

Abbreviations: ECM—extracellular matrix, ABS—actin binding site, DLC1—liver tumor suppressor, FAK—focal adhesion kinase, FERM—family of proteins (protein 4.1, ezrin, radixin, moesin), IBS—integrin binding site, KANK1-2—kidney ankyrin repeat-containing proteins, PIP2—phosphatidylinositol 4,5-bisphosphate, PIPK1γ—phosphatidylinositol 4-phosphate 5-kinase type I, RIAM—Rap1-GTP-interacting adapter molecule, TIAM1—T-cell lymphoma invasion and metastasis inducing factor; VBS,—vinculin binding site.

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Ivanova, V.P. Talin: Structural and Functional Relationships. Cell Tiss. Biol. 15, 416–427 (2021). https://doi.org/10.1134/S1990519X21050060

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