Inhibition of dendritic spine extension through acrolein conjugation with α-, β-tubulin proteins

Uemura, Takeshi; Suzuki, Takehiro; Ko, Kenta; Watanabe, Kenta; Dohmae, Naoshi; Sakamoto, Akihiko; Terui, Yusuke; Toida, Toshihiko; Kashiwagi, Keiko; Igarashi, Kazuei

doi:10.1016/j.biocel.2019.05.016

Cited by 14 publications

(14 citation statements)

References 33 publications

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“…Time course observation of vimentin and actin in acrolein treated cells revealed that vimentin in the dendritic spines diminished then aggregation of vimentin followed (Figure 4). This was confirmed in brain tissue: acrolein conjugation As for the acrolein-conjugated amino acid residues involved in the activities, for GAPDH it was Cys150 (Nakamura et al, 2013), with MMP-9 it was Cys99 (Uemura et al, 2017), and for αand β-tubulins they were Cys25, 295, 347, and 376 in α-tubulin, and Cys12, 129, 211, 239, 303, and 354 in β-tubulin (Uemura et al, 2019). In the case of vimentin and actin, they were Cys328 for vimentin, and Cys207, 257, 285, and Lys118 for actin, respectively.…”

Section: Structural Change Of Intermediate Filament and Microfilamementioning

confidence: 60%

“…Since both microtubule consisting of αand β-tubulins and intermediate filament consisting of vimentin were conjugated with acrolein ((Uemura et al, 2019) and Figure 2), it was tested whether acrolein is conjugated with actin, another protein consisting microfilament, using purified actin. As shown in Figure 3, Cys217,257,285,and Lys118 were conjugated with acrolein.…”

Section: Identification Of Acrolein-conjugated Amino Acid Residues mentioning

confidence: 99%

“…At the molecular level, the tissue damage is caused by inactivation of GAPDH (Nakamura et al, 2013), and activation of MMP-9 (Uemura et al, 2017) through conjugation with acrolein. In the course of studying the molecular mechanism of acrolein toxicity in brain stroke, we have found that αand β-tubulin proteins were substantially conjugated with acrolein in infarct brain (Uemura et al, 2019). Since it has been reported that microtubules are important for normal brain function (Janke & Bulinski, 2011;Pchitskaya, Zhemkov, & Bezprozvanny, 2018), we have studied the effect of acrolein on the structure of microtubules consisting of αand β-tubulins (Uemura et al, 2019).…”

Section: Structural Change Of Intermediate Filament and Microfilamementioning

confidence: 99%

“…In the course of studying the molecular mechanism of acrolein toxicity in brain stroke, we have found that αand β-tubulin proteins were substantially conjugated with acrolein in infarct brain (Uemura et al, 2019). Since it has been reported that microtubules are important for normal brain function (Janke & Bulinski, 2011;Pchitskaya, Zhemkov, & Bezprozvanny, 2018), we have studied the effect of acrolein on the structure of microtubules consisting of αand β-tubulins (Uemura et al, 2019). It was shown that acrolein conjugation strongly inhibited polymerization of αand β-tubulin proteins and dendritic spine extension.…”

Section: Structural Change Of Intermediate Filament and Microfilamementioning

confidence: 99%

“…With regard to acrolein toxicity, we found that acroleinconjugated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) translocated to the nucleus and caused apoptosis in mouse mammary carcinoma FM3A cells (Nakamura et al, 2013), and that acrolein stimulated matrix metalloproteinase (MMP)-9 activity in saliva from patients with primary Sjögren's syndrome leading to tissue damage (Uemura et al, 2017). It was also found that dendritic spine extension was inhibited through acrolein conjugation with αand β-tubulin proteins in neuroblastoma Neuro2a cells and PIT model mice (Uemura et al, 2019). The acrolein conjugation strongly inhibited polymerization of αand β-tubulins into microtubules and drastically changed the morphology of cells.…”

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confidence: 99%

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Structural change and degradation of cytoskeleton due to the acrolein conjugation with vimentin and actin during brain infarction

Uemura

Suzuki

et al. 2020

Cytoskeleton

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We have found recently that dendritic spine extension is inhibited through acrolein conjugation with αand β-tubulin proteins during brain infarction. In this current study, we looked for other acrolein-conjugated proteins in the 100,000g precipitate fraction, to clarify how cytoskeleton structure is modified by acrolein. Acroleinconjugated proteins were sought from acrolein-treated mouse FM3A and Neuro2a cells and from tissues isolated from mouse brain infarction. It was found that vimentin was conjugated with acrolein, and the conjugated amino acid residue was Cys328, which is the only Cys residue in vimentin. It was also found that Cys207, 257, 285, and Lys118 in actin, another cytoskeleton protein, were conjugated with acrolein. The structure and localization of vimentin and actin filaments were changed greatly in infarct brain in photochemically induced thrombosis model mice and in acrolein-treated Neuro2a cells. In addition, degradation of cytoskeleton proteins was accelerated in the order vimentin > tubulin > actin in mouse brain infarction. These findings indicate that a dysfunction of the cytoskeleton by acrolein is strongly involved in the tissue damage during brain infarction, together with the apoptosis caused by glyceraldehyde-3-phosphate dehydrogenase and protein degradation by matrix metalloproteinase-9.

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Section: Structural Change Of Intermediate Filament and Microfilamementioning

confidence: 60%

Section: Identification Of Acrolein-conjugated Amino Acid Residues mentioning

confidence: 99%

Section: Structural Change Of Intermediate Filament and Microfilamementioning

confidence: 99%

Section: Structural Change Of Intermediate Filament and Microfilamementioning

confidence: 99%

mentioning

confidence: 99%

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Structural change and degradation of cytoskeleton due to the acrolein conjugation with vimentin and actin during brain infarction

Uemura

Suzuki

et al. 2020

Cytoskeleton

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Positional cloning identified HvTUBULIN8 as the candidate gene for round lateral spikelet (RLS) in barley (Hordeum vulgare L.)

Qin

Liu

et al. 2023

Theor Appl Genet

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Key message Map-based cloning, subcellular localization, virus-induced-gene-silencing and transcriptomic analysis reveal HvTUB8 as a candidate gene with pleiotropic effects on barley spike and leaf development via ethylene and chlorophyll metabolism. Abstract Barley lateral spikelet morphology and grain shape play key roles in grain physical quality and yield. Several genes and QTLs for these traits have been cloned or fine mapped previously. Here, we report the phenotypic and genotypic analysis of a barley mutant with round lateral spikelet (rls) from cv. Edamai 934. rls had round lateral spikelet, short but round grain, shortened awn, thick glume and dark green leaves. Histocytologic and ultrastructural analysis revealed that the difference of grain shape of rls was caused by change of cell arrangement in glume, and the dark leaf color resulted from enlarged chloroplast. HvTUBULIN8 (HvTUB8) was identified as the candidate gene for rls by combination of RNA-Seq, map-based-cloning, virus-induced-gene-silencing (VIGS) and protein subcellular location. A single G-A substitution at the third exon of HvTUB8 resulted in change of Cysteine 354 to tyrosine. Furthermore, the mutant isoform Hvtub8 could be detected in both nucleus and cytoplasm, whereas the wild-type protein was only in cytoplasm and granular organelles of wheat protoplasts. Being consistent with the rare phenotype, the “A” allele of HvTUB8 was only detected in rls, but not in a worldwide barley germplasm panel with 400 accessions. VIGS confirmed that HvTUB8 was essential to maintain spike integrity. RNA-Seq results suggested that HvTUB8 may control spike morphogenesis via ethylene homeostasis and signaling, and control leaf color through chlorophyll metabolism. Collectively, our results support HvTUB8 as a candidate gene for barley spike and leaf morphology and provide insight of a novel mechanism of it in barley development.

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Functional roles of polyamines and their metabolite acrolein in eukaryotic cells

Igarashi

Kashiwagi

2021

Amino Acids

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Inhibition of dendritic spine extension through acrolein conjugation with α-, β-tubulin proteins

Cited by 14 publications

References 33 publications

Structural change and degradation of cytoskeleton due to the acrolein conjugation with vimentin and actin during brain infarction

Structural change and degradation of cytoskeleton due to the acrolein conjugation with vimentin and actin during brain infarction

Positional cloning identified HvTUBULIN8 as the candidate gene for round lateral spikelet (RLS) in barley (Hordeum vulgare L.)

Functional roles of polyamines and their metabolite acrolein in eukaryotic cells

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