Transcription-dependent rearrangements of actin and nuclear myosin I in the nucleolus

Philimonenko, Vlada; Janáček, Jiřı́; Harata, Masahiko; Hozák, Pavel

doi:10.1007/s00418-010-0732-8

Cited by 28 publications

(20 citation statements)

References 36 publications

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“…The results were in line with the dynamic behaviour of NMI and its role in rDNA transcription (Percipalle et al 2006;Philimonenko et al 2010), through concentration of NMI mainly in the dense Wbrillar component (DFC) of actively transcribing nucleoli and co-localization with nascent transcripts. However, the studies also revealed, due to the observation of an NMI fraction that did not associate with rDNA transcription, additional roles of NMI in other nucleolar processes (e.g.…”

Section: Moleculessupporting

confidence: 81%

“…An ultrastructural analysis of the nucleolar spatial arrangement of actin and nuclear myosin I (NMI) was performed by Philimonenko et al (2010) to derive functional implications. The results were in line with the dynamic behaviour of NMI and its role in rDNA transcription (Percipalle et al 2006;Philimonenko et al 2010), through concentration of NMI mainly in the dense Wbrillar component (DFC) of actively transcribing nucleoli and co-localization with nascent transcripts.…”

Section: Moleculesmentioning

confidence: 99%

See 1 more Smart Citation

Histochemistry and cell biology: the annual review 2010

Hübner

Efthymiadis

2011

Histochem Cell Biol

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This review summarizes recent advances in histochemistry and cell biology which complement and extend our knowledge regarding various aspects of protein functions, cell and tissue biology, employing appropriate in vivo model systems in conjunction with established and novel approaches. In this context several non-expected results and discoveries were obtained which paved the way of research into new directions. Once the reader embarks on reading this review, it quickly becomes quite obvious that the studies contribute not only to a better understanding of fundamental biological processes but also provide use-oriented aspects that can be derived therefrom.

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Section: Moleculessupporting

confidence: 81%

Section: Moleculesmentioning

confidence: 99%

Histochemistry and cell biology: the annual review 2010

Hübner

Efthymiadis

2011

Histochem Cell Biol

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“…These reports strongly suggest that the functions of nuclear myosins differ from that of cytoplasmic myosins. Indeed, nuclear myosin I was found to mediate the transcription of ribosomal RNA genes through cooperation with nuclear actin [23,25]; whereas nuclear myosin (II) was reported to function as a transcription factor in colonic smooth muscle cells to regulate the protein-coding genes (such as ICAM-1) and its transcriptional activity is dependent on the phosphorylation status of MLC 20 [16]. In the present study, we provide evidence for the first time that MYL2 localizes in both cytoplasm and nucleus of cardiomyocyte.…”

Section: Discussionmentioning

confidence: 99%

Nuclear cardiac myosin light chain 2 modulates NADPH oxidase 2 expression in myocardium: a novel function beyond muscle contraction

et al. 2015

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Recent studies demonstrated that NADPH oxidase 2 (NOX2) expression in myocardium after ischemia-reperfusion (IR) is significantly upregulated. However, the underlying mechanisms remain unknown. This study aims to determine if nuclear cardiac myosin light chain 2 (MYL2), a well-known regulatory subunit of myosin, functions as a transcription factor to promote NOX2 expression following myocardial IR in a phosphorylation-dependent manner. We examined the phosphorylation status of nuclear MYL2 (p-MYL2) in a rat model of myocardial IR (left main coronary artery subjected to 1 h ligation and 3 h reperfusion) injury, which showed IR injury and upregulated NOX2 expression as expected, accompanied by elevated H₂O₂ and nuclear p-MYL2 levels; these effects were attenuated by inhibition of myosin light chain kinase (MLCK). Next, we explored the functional relationship of nuclear p-MYL2 with NOX2 expression in H9c2 cell model of hypoxia-reoxygenation (HR) injury. In agreement with our in vivo findings, HR treatment increased apoptosis, NOX2 expression, nuclear p-MYL2 and H₂O₂ levels, and the increases were ameliorated by inhibition of MLCK or knockdown of MYL2. Finally, molecular biology techniques including co-immunoprecipitation (Co-IP), chromatin immunoprecipitation (ChIP), DNA pull-down and luciferase reporter gene assay were utilized to decipher the molecular mechanisms. We found that nuclear p-MYL2 binds to the consensus sequence AGCTCC in NOX2 gene promoter, interacts with RNA polymerase II and transcription factor IIB to form a transcription preinitiation complex, and thus activates NOX2 gene transcription. Our results demonstrate that nuclear MYL2 plays an important role in IR injury by transcriptionally upregulating NOX2 expression to enhance oxidative stress in a phosphorylation-dependent manner.

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“…They are involved in vesicle trafficking (Yokota et al, 1995) and transcription of ribosomal proteins (Philimonenko et al, 2010). The myosin heavy-chain protein subunit is saltresponsive and is directly influenced by the vacuolar Na + /H + antiporter that mediates transport of Na + and K + into the vacuole (Sottosanto et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Protein Expression After Nacl Treatment in Two Tomato Cultivars Differing in Salt Tolerance

Khalifa¹

2012

Acta Biologica Cracoviensia Series Botanica

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SDS-PAGE electrophoresis was used to study the effect of NaCl on protein expression in two cultivars of tomato (Solanum lycopersicum L.): Edkawi (salt-tolerant) and Castle rock (salt-sensitive). Five-day-old seedlings were grown on MS agar media supplemented with 0, 50, 100, 150, 200 and 300 mM NaCl. Two days after treatment the seedlings were examined to determine the effect of salt on their growth and to relate that to protein banding variations. Gel analysis showed differences in at least 4 protein bands with molecular weights at 20, 25, 45 and 65 kDa. These proteins were induced in the 50 mM NaCl treatment in the salt-sensitive cultivar, then decreasing to undetectability at higher concentrations. In the salt-tolerant cultivar, most of the proteins exhibited a more or less steady expression pattern and maintained expression through the 200 mM NaCl treatment. All proteins gave weak or no expression signals at 300 mM NaCl, the treatment that proved lethal. Differentially expressed bands were identified using MALDI-TOF mass spectrometry. The putative function of each identified protein in relation to salt stress is discussed.K Ke ey y w wo or rd ds s: : SDS-PAGE, salinity, 45 S ribosomal protein, Rubisco, MALDI-TOF mass spectrometry, tomato.

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Transcription-dependent rearrangements of actin and nuclear myosin I in the nucleolus

Cited by 28 publications

References 36 publications

Histochemistry and cell biology: the annual review 2010

Histochemistry and cell biology: the annual review 2010

Nuclear cardiac myosin light chain 2 modulates NADPH oxidase 2 expression in myocardium: a novel function beyond muscle contraction

Protein Expression After Nacl Treatment in Two Tomato Cultivars Differing in Salt Tolerance

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