Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode

Jodi Kraus, Ryan W. Russell, Elena Kudryashova, Chaoyi Xu, Nidhi Katyal, Juan R. Perilla, Dmitri S. Kudryashov and Tatyana Polenova ()
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Jodi Kraus: University of Delaware
Ryan W. Russell: University of Delaware
Elena Kudryashova: The Ohio State University
Chaoyi Xu: University of Delaware
Nidhi Katyal: University of Delaware
Juan R. Perilla: University of Delaware
Dmitri S. Kudryashov: The Ohio State University
Tatyana Polenova: University of Delaware

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract Actin polymerization dynamics regulated by actin-binding proteins are essential for various cellular functions. The cofilin family of proteins are potent regulators of actin severing and filament disassembly. The structural basis for cofilin-isoform-specific severing activity is poorly understood as their high-resolution structures in complex with filamentous actin (F-actin) are lacking. Here, we present the atomic-resolution structure of the muscle-tissue-specific isoform, cofilin-2 (CFL2), assembled on ADP-F-actin, determined by magic-angle-spinning (MAS) NMR spectroscopy and data-guided molecular dynamics (MD) simulations. We observe an isoform-specific conformation for CFL2. This conformation is the result of a unique network of hydrogen bonding interactions within the α2 helix containing the non-conserved residue, Q26. Our results indicate F-site interactions that are specific between CFL2 and ADP-F-actin, revealing mechanistic insights into isoform-dependent F-actin disassembly.

Date: 2022
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DOI: 10.1038/s41467-022-29595-9

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