Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II

Snijder, Joost; Rose, Rebecca; Raijmakers, Reinout; Heck, Albert J. R.

doi:10.1016/j.jsb.2010.12.002

Cited by 33 publications

(29 citation statements)

References 45 publications

(81 reference statements)

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“…This is true, in particular, for cholera, whose secretory diarrhea depends on the CFTR chloride and SK potassium channels, both of which are calmodulin-dependent [45, 46]. Calmodulin is a Ca 2+ - binding regulatory molecule, which becomes unresponsive to Ca 2+ activation upon oxidation of methionines 144 and 145 [47, 48]. Function is restored when these methionines are reduced by MsrA [49, 50].…”

Section: Discussionmentioning

confidence: 99%

Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide

et al. 2017

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Vibrio cholerae is a diarrheal pathogen that induces accumulation of lipid droplets in enterocytes, leading to lethal infection of the model host Drosophila melanogaster. Through untargeted lipidomics, we provide evidence that this process is the product of a host phospholipid degradation cascade that induces lipid droplet coalescence in enterocytes. This infection-induced cascade is inhibited by mutation of the V. cholerae glycine cleavage system due to intestinal accumulation of methionine sulfoxide (MetO), and both dietary supplementation with MetO and enterocyte knock-down of host methionine sulfoxide reductase A (MsrA) yield increased resistance to infection. MsrA converts both free and protein-associated MetO to methionine. These findings support a model in which dietary MetO competitively inhibits repair of host proteins by MsrA. Bacterial virulence strategies depend on functional host proteins. We propose a novel virulence paradigm in which an intestinal pathogen ensures the repair of host proteins essential for pathogenesis through consumption of dietary MetO.

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Section: Discussionmentioning

confidence: 99%

Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide

et al. 2017

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“…A mouse mutant lacking msrA showed increased CaMKII oxidation and exacerbation of the effect of myocardial infarction. In a related study, Snijder et al (2011) showed that oxidation of Met144 and 145 in CaM inhibits interaction with CaMKII. Although no phosphorylation is involved in this instance, Met oxidation affects the kinase recognition.…”

Section: Crosstalk Between Met Oxidation and O-phosphorylationmentioning

confidence: 97%

“…1). Second, oxidation of Met in a cohort protein (e.g., CaM) might inhibit recognition/binding of the kinase to the client protein (Snijder et al 2011). Finally, there might be oxidation of a Met in the kinase sequence itself (for example, CaMKII) which affects activity or signaling efficiency (Cao et al 2010;Erickson et al 2008).…”

Section: Crosstalk Between Met Oxidation and O-phosphorylationmentioning

confidence: 99%

Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Rao

Thelen

Miernyk

2015

Cell Stress and Chaperones

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Oxidation of methionine (Met) to Met sulfoxide (MetSO) is a frequently found reversible posttranslational modification. It has been presumed that the major functional role for oxidation-labile Met residues is to protect proteins/ cells from oxidative stress. However, Met oxidation has been established as a key mechanism for direct regulation of a wide range of protein functions and cellular processes. Furthermore, recent reports suggest an interaction between Met oxidation and O-phosphorylation. Such interactions are a potentially direct interface between redox sensing and signaling, and cellular protein kinase/phosphatase-based signaling. Herein, we describe the current state of Met oxidation research, provide some mechanistic insight into crosstalk between these two major posttranslational modifications, and consider the evolutionary significance and regulatory potential of this crosstalk.

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“…Oxidation of Met was reported to occur in various signaling proteins, thereby modulating their functions [1–9]. For example, calmodulin (CAM), a versatile protein involved in various signaling pathways, including ROS homeostasis in Arabidopsis [10], is well known to have its methionine residue oxidation linked to protein dysfunction [11] and loss of protein stability [12]. Nevertheless, efforts to systematically identify all the proteins whose methionine residues are susceptible to oxidation yielded limited results due to the lack of viable tools, including an antibody specific to methionine sulfoxide [13–16].…”

Section: Introductionmentioning

confidence: 99%

“…This study also suggested a list of potential substrates of AtMSRB7. Despite the fact that oxidation and reduction of Met residues in CAM and other calcium signaling proteins were experimentally verified to be involved in regulating the protein's functions [2–4, 11, 12], they were not found among the potential candidates acquired by either the affinity chromatography approach or approaches that employed mass spectroscopy [17, 19, 29]. This line of evidence offers opportunity to argue that either the current approaches for proteome-wide identification of MSR targets pose technical limitations or the oxidation and reduction of Met in many proteins like CAM happen transiently, such that these techniques were unable to help in identifying them.…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Analysis of Genes Encoding Methionine-Rich Proteins inArabidopsisand Soybean Suggesting Their Roles in the Adaptation of Plants to Abiotic Stress

Chu

Nguyen

et al. 2016

International Journal of Genomics

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Oxidation and reduction of methionine (Met) play important roles in scavenging reactive oxygen species (ROS) and signaling in living organisms. To understand the impacts of Met oxidation and reduction in plants during stress, we surveyed the genomes of Arabidopsis and soybean (Glycine max L.) for genes encoding Met-rich proteins (MRPs). We found 121 and 213 genes encoding MRPs in Arabidopsis and soybean, respectively. Gene annotation indicated that those with known function are involved in vital cellular processes such as transcriptional control, calcium signaling, protein modification, and metal transport. Next, we analyzed the transcript levels of MRP-coding genes under normal and stress conditions. We found that 57 AtMRPs were responsive either to drought or to high salinity stress in Arabidopsis; 35 GmMRPs were responsive to drought in the leaf of late vegetative or early reproductive stages of soybean. Among the MRP genes with a known function, the majority of the abiotic stress-responsive genes are involved in transcription control and calcium signaling. Finally, Arabidopsis plant which overexpressed an MRP-coding gene, whose transcripts were downregulated by abiotic stress, was more sensitive to paraquat than the control. Taken together, our report indicates that MRPs participate in various vital processes of plants under normal and stress conditions.

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Site-specific methionine oxidation in calmodulin affects structural integrity and interaction with Ca2+/calmodulin-dependent protein kinase II

Cited by 33 publications

References 45 publications

Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide

Vibrio cholerae ensures function of host proteins required for virulence through consumption of luminal methionine sulfoxide

Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Genome-Wide Analysis of Genes Encoding Methionine-Rich Proteins inArabidopsisand Soybean Suggesting Their Roles in the Adaptation of Plants to Abiotic Stress

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