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- 저자 : Rubinsztein, David C. (검색결과 6 건)
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Autophagy, Cellular Aging and Age-related Human Diseases
전소영,김현정,David C. Rubinsztein,이종은 한국뇌신경과학회 2019 Experimental Neurobiology Vol.28 No.6
Macroautophagy/autophagy is a conserved degradation system that engulfs intracytoplasmic contents, including aggregated proteins and organelles, which is crucial for cellular homeostasis. During aging, cellular factors suggested as the cause of aging have been reported to be associated with progressively compromised autophagy. Dysfunctional autophagy may contribute to age-related diseases, such as neurodegenerative disease, cancer, and metabolic syndrome, in the elderly. Therefore, restoration of impaired autophagy to normal may help to prevent age-related disease and extend lifespan and longevity. Therefore, this review aims to provide an overview of the mechanisms of autophagy underlying cellular aging and the consequent disease. Understanding the mechanisms of autophagy may provide potential information to aid therapeutic interventions in age-related diseases.
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Transcriptional regulation of mammalian autophagy at a glance
Fullgrabe, Jens,Ghislat, Ghita,Cho, Dong-Hyung,Rubinsztein, David C. The Company of Biologists Ltd. 2016 Journal of cell science Vol.129 No.16
<P>Macroautophagy, hereafter referred to as autophagy, is a catabolic process that results in the lysosomal degradation of cytoplasmic contents ranging from abnormal proteins to damaged cell organelles. It is activated under diverse conditions, including nutrient deprivation and hypoxia. During autophagy, members of the core autophagy-related (ATG) family of proteins mediate membrane rearrangements, which lead to the engulfment and degradation of cytoplasmic cargo. Recently, the nuclear regulation of autophagy, especially by transcription factors and histone modifiers, has gained increased attention. These factors are not only involved in rapid responses to autophagic stimuli, but also regulate the long-term outcome of autophagy. Now there are more than 20 transcription factors that have been shown to be linked to the autophagic process. However, their interplay and timing appear enigmatic as several have been individually shown to act as major regulators of autophagy. This Cell Science at a Glance article and the accompanying poster highlights the main cellular regulators of transcription involved in mammalian autophagy and their target genes.</P>
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Autophagy regulation by acetylation—implications for neurodegenerative diseases
Son Sung Min,Park So Jung,Fernandez-Estevez Marian,Rubinsztein David C. 생화학분자생물학회 2021 Experimental and molecular medicine Vol.53 No.-
Posttranslational modifications of proteins, such as acetylation, are essential for the regulation of diverse physiological processes, including metabolism, development and aging. Autophagy is an evolutionarily conserved catabolic process that involves the highly regulated sequestration of intracytoplasmic contents in double-membrane vesicles called autophagosomes, which are subsequently degraded after fusing with lysosomes. The roles and mechanisms of acetylation in autophagy control have emerged only in the last few years. In this review, we describe key molecular mechanisms by which previously identified acetyltransferases and deacetylases regulate autophagy. We highlight how p300 acetyltransferase controls mTORC1 activity to regulate autophagy under starvation and refeeding conditions in many cell types. Finally, we discuss how altered acetylation may impact various neurodegenerative diseases in which many of the causative proteins are autophagy substrates. These studies highlight some of the complexities that may need to be considered by anyone aiming to perturb acetylation under these conditions.
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A PbS quantum-cube: conducting polymer composite for photovoltaic applications
A. A. R. Watt,P. Meredith,J. D. Riches,S. Atkinson,H. Rubinsztein-Dunlop 한국물리학회 2004 Current Applied Physics Vol.4 No.2-4
We have developed a new non-polar synthesis for lead sulde (PbS) ‘‘quantum-cubes’’ in the conjugated polymer poly-2-methoxy,5-(2-ethyl-hexyloxy-p-phenylenevinylene) MEH-PPV. The conducting polymer acts to template and control the quantum-cube growth. Transmission electron microscopy of the composites has shown a bimodal distribution of cube sizes between 5 and 15nm is produced with broad optical absorption from 300 to 650 nm. Photoluminescence suggests electronic coupling between thecubes and the conducting polymer matrix. The synthesis and initial characterization are presented in this paper.
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Park, So Jung,Lee, Heejin,Jo, Doo Shin,Jo, Yoon Kyung,Shin, Ji Hyun,Kim, Han Byeol,Seo, Hae Mi,Rubinsztein, David C.,Koh, Jae-Young,Lee, Eun Kyung,Cho, Dong-Hyung Elsevier Pub. Co 2015 Biochimica et biophysica acta. Gene regulatory mec Vol.1849 No.12
<▼1><P>Excessive mitochondrial fission is associated with the pathogenesis of neurodegenerative diseases. Dynamin-related protein 1 (Drp1) possesses specific fission activity in the mitochondria and peroxisomes. Various post-translational modifications of Drp1 are known to modulate complex mitochondrial dynamics. However, the post-transcriptional regulation of Drp1 remains poorly understood. Here, we show that the heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) regulates Drp1 expression at the post-transcriptional level. hnRNP A1 directly interacts with Drp1 mRNA at its 3′UTR region, and enhances translation potential without affecting mRNA stability. Down-regulation of hnRNP A1 induces mitochondrial elongation by reducing Drp1 expression. Moreover, depletion of hnRNP A1 suppresses 3-NP-mediated mitochondrial fission and dysfunction. In contrast, over-expression of hnRNP A1 promotes mitochondrial fragmentation by increasing Drp1 expression. Additionally, hnRNP A1 significantly exacerbates 3-NP-induced mitochondrial dysfunction and cell death in neuroblastoma cells. Interestingly, treatment with 3-NP induces subcellular translocation of hnRNP A1 from the nucleus to the cytoplasm, which accelerates the increase in Drp1 expression in hnRNP A1 over-expressing cells. Collectively, our findings suggest that hnRNP A1 controls mitochondrial dynamics by post-transcriptional regulation of Drp1.</P></▼1><▼2><P><B>Highlights</B></P><P>•<P>hnRNP A1 increases Drp1 expression through the interaction with 3′UTR of Drp1 mRNA.</P>•<P>Down-regulation of hnRNP A1 increases mitochondrial elongation by reducing drp1 expression.</P>•<P>Down-regulation of hnRNPA1 inhibits 3-NP-mediated mitochondrial dysfunction.</P>•<P>Over-expression of hnRNP A1 potentiates 3-NP-mediated mitochondrial dysfunction and cell death.</P>•<P>Treatment of 3-NP promotes translocation of hnRNP A1 to the cytoplasm and enhances Drp1 expression.</P></P></▼2>
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