2019
DOI: 10.1002/cm.21520
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S‐nitrosylation of cytoskeletal proteins

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 guanosine monophosphate (cGMP), 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 e… Show more

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Cited by 20 publications
(23 citation statements)
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References 112 publications
(158 reference statements)
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“…The accumulating data show that the SNO of cytoskeletal proteins selectively alters their function. It complements the effects of cGMP on cytoskeletal proteins in the cells, modulating cell migration and contractility [11]. Accordingly, it has been shown that the proteostasis of actin and tubulin proteins is precisely controlled during neuronal maturation in the brain, and NO signaling appears to be a key regulator of these processes [63].…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The accumulating data show that the SNO of cytoskeletal proteins selectively alters their function. It complements the effects of cGMP on cytoskeletal proteins in the cells, modulating cell migration and contractility [11]. Accordingly, it has been shown that the proteostasis of actin and tubulin proteins is precisely controlled during neuronal maturation in the brain, and NO signaling appears to be a key regulator of these processes [63].…”
Section: Discussionmentioning
confidence: 99%
“…At some cysteines, it can be driven by a putative "nitrosylation motif" in the primary structure of Biomedicines 2020, 8, 124 2 of 20 nitrosoproteins [8,10]. Such motifs could be incorporated into the three-dimensional structure of cysteines rather than in the primary structure [11]. SNO plays a signaling role in regulation of protein localization, axonal transport, synaptic plasticity and various neuronal pathways [12,13].…”
Section: Introductionmentioning
confidence: 99%
“…NO bioactivity has also been associated with sGC‐independent effects, via covalent post‐translational modification of target proteins including S‐nitrosylation (ie binding of a NO group to a transition metal or cysteine residues and forming an nitrosothiol moiety), as well as tyrosine nitration (ie binding of a NO 2 group to a tyrosine or tryptophan residue) of proteins as well as unsaturated fatty acids . Although some physiological roles have been reported for S‐nitrosylation, sGC‐independent effects mainly occur at high concentrations (ie µmol L −1 ‐mmol L −1 range) of NO and mostly mediate its detrimental effects . This issue is unlike sGC‐dependent physiological effects of NO which occur in the presence of low nanomolar concentrations of NO …”
Section: No Receptormentioning
confidence: 99%
“…Of note, another common target of NO and CyPG is the actin cytoskeleton. An increasing number of studies have identified actin and actin-binding proteins (ABPs) as major targets of RNS and CyPG in both physiological and oxidative pathophysiological conditions, resulting in alterations of actin network rearrangements by disturbing filament growth and stabilization (Gayarre et al, 2006;Horenberg et al, 2019;Varland et al, 2019).…”
Section: Introductionmentioning
confidence: 99%