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Aravinth kumar Jayabalan,Takbum Ohn 대한의생명과학회 2014 Biomedical Science Letters Vol.20 No.1
RNA granules such as Stress Granules (SG) and P-Bodies (PB) are aggregates of translationally stalled messenger ribonucleoprotein (mRNP) complexes induced by a wide range of stresses. Over the past decade, extensive studies described key components of RNA granules, their molecular interactions and signaling pathways require for their assembly and disassembly. However, researches defining their exact roles under stress conditions have not been performed so far, although several studies suggested their roles in neurodegenerative diseases recently. In this review, we provide an introduction about their basic properties, key components, and the dynamic nature for their assembly.
Identification of Neuregulin-2 as a novel stress granule component
( Jin Ah Kim ),( Aravinth Kumar Jayabalan ),( Vinoth Kumar Kothandan ),( Ramesh Mariappan ),( Younghoon Kee ),( Takbum Ohn ) 생화학분자생물학회(구 한국생화학분자생물학회) 2016 BMB Reports Vol.49 No.8
Stress Granules (SGs) are microscopically visible, phase dense aggregates of translationally stalled messenger ribonucleoprotein (mRNP) complexes formed in response to distinct stress conditions. It is generally considered that SG formation is induced to protect cells from conditions of stress. The precise constituents of SGs and the mechanism through which SGs are dynamically regulated in response to stress are not completely understood. Hence, it is important to identify proteins which regulate SG assembly and disassembly. In the present study, we report Neuregulin-2 (NRG2) as a novel component of SGs; furthermore, depletion of NRG2 potently inhibits SG formation. We also demonstrate that NRG2 specifically localizes to SGs under various stress conditions. Knockdown of NRG2 has no effect on stress-induced polysome disassembly, suggesting that the component does not influence early step of SG formation. It was also observed that reduced expression of NRG2 led to marginal increase in cell survival under arsenite-induced stress. [BMB Reports 2016; 49(8): 449-454]
miR-27 regulates mitochondrial networks by directly targeting the mitochondrial fission factor
Tak, Hyosun,Kim, Jihye,Jayabalan, Aravinth Kumar,Lee, Heejin,Kang, Hoin,Cho, Dong-Hyung,Ohn, Takbum,Nam, Suk Woo,Kim, Wook,Lee, Eun Kyung Nature Publishing Group 2014 Experimental and molecular medicine Vol.46 No.11
<P>Mitochondrial morphology is dynamically regulated by forming small, fragmented units or interconnected networks, and this is a pivotal process that is used to maintain mitochondrial homeostasis. Although dysregulation of mitochondrial dynamics is related to the pathogenesis of several human diseases, its molecular mechanism is not fully elucidated. In this study, we demonstrate the potential role of miR-27 in the regulation of mitochondrial dynamics. <I>Mitochondrial fission factor</I> (<I>MFF</I>) mRNA is a direct target of miR-27, whose ectopic expression decreases MFF expression through binding to its 3′-untranslated region. Expression of miR-27 results in the elongation of mitochondria as well as an increased mitochondrial membrane potential and mitochondrial ATP level. Our results suggest that miR-27 is a novel regulator affecting morphological mitochondrial changes by targeting MFF.</P>
miR-27 regulates mitochondrial networks by directly targeting the mitochondrial fission factor
탁효선,이은경,김지혜,남석우,이희진,Aravinth kumar Jayabalan,강호인,조동형,온탁범,김욱 생화학분자생물학회 2014 Experimental and molecular medicine Vol.46 No.-
Mitochondrial morphology is dynamically regulated by forming small, fragmented units or interconnected networks, and this is a pivotal process that is used to maintain mitochondrial homeostasis. Although dysregulation of mitochondrial dynamics is related to the pathogenesis of several human diseases, its molecular mechanism is not fully elucidated. In this study, we demonstrate the potential role of miR-27 in the regulation of mitochondrial dynamics. Mitochondrial fission factor (MFF) mRNA is a direct target of miR-27, whose ectopic expression decreases MFF expression through binding to its 3′-untranslated region. Expression of miR-27 results in the elongation of mitochondria as well as an increased mitochondrial membrane potential and mitochondrial ATP level. Our results suggest that miR-27 is a novel regulator affecting morphological mitochondrial changes by targeting MFF.