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S-nitrosylation of cytoskeletal proteins.

Research paper by Allison L AL Horenberg, Alisa M AM Houghton, Saurav S Pandey, Vikram V Seshadri, William H WH Guilford

Indexed on: 08 Jul '19Published on: 11 Apr '19Published in: Cytoskeleton



Abstract

Nitric oxide has pronounced effects on cellular functions normally associated with the cytoskeleton, including cell motility, shape, contraction, and mitosis. Protein S-nitrosylation, the covalent addition of a NO group to a cysteine sulfur, is a signaling pathway for nitric oxide that acts in parallel to cyclic-GMP, but is poorly studied compared to the latter. There is growing evidence that S-nitrosylation of cytoskeletal proteins selectively alters their function. We review that evidence, and find that S-nitrosylation of cytoskeletal targets has complementary but distinct effects to cyclic-GMP in motile and contractile cells - promoting cell migration, and biasing muscle contraction toward relaxation. However, the effects of S-nitrosylation on a host of cytoskeletal proteins and functions remains to be explored. This article is protected by copyright. All rights reserved. © 2019 Wiley Periodicals, Inc.