• Title/Summary/Keyword: dynamin

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Up-regulation of dynamin-2 gene expression in Ras-transformed cells (Ras에 의해 암화된 세포에서 dynamin-2의 발현 촉진)

  • Yoo, Ji-Yun
    • Journal of Life Science
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    • v.17 no.3 s.83
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    • pp.375-380
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    • 2007
  • Dynamin plays a key role in the scission event common to various types of endocytosis. It has been previously reported that the SH3 domain-mediated association of Grb2 with dynamin-2 was dominantly found in Ras transformed cells. However, whether this association results from the increased expression of dynamin-2 and Grb2 in Ras transformed cells or not is still unknown. So in this study we first analyzed the expression levels of dynamin-2 and Grb2 and found that the expression of dynamin-2 protein was dramatically increased in Ras-transformed NIH3T3 (NIH3T3(Ras)) cells. Furthermore competitive PCR data revealed that the mRNA transcripts for dynamin-2 were increased about 100-fold in NIH3T3(Ras) compared to those of NIH3T3 cells. However, the protein level and mRNA transcript of Grb2 were not changed in these two cells. We also examined promoter activity of dynamin-2 in NIH3T3(Ras) cells and suggest the existence of Ras-responsive sequence in promoter region -300 to -200.

Dynamin II Expression and Morphological Comparison of NIH3T3 and NIH3T3 (ras) Cells (NIH3T3와 NIH3T3(ras) 세포에서 Dynamin II 발현 및 형태적 비교)

  • Lee, Chul-Woo;Kim, Su-Gwan;Choi, Jeong-Yun;Choi, Baik-Dong;Bae, Chun-Sik;Jeong, Soon-Jeong;Jeong, Moon-Jin
    • Applied Microscopy
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    • v.35 no.3
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    • pp.121-128
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    • 2005
  • It has been known that ras signaling transduction leads to cell proliferation and migration including various adaptor molecules. Dynamin protein has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. Dynamin was classified into three isoforms: dynamin I is only expressed in neuronal tissue, dynamin II is expressed ubiquitously in all tissue but that of dynamin III is confined to testis. We have reported in previous study that Grb2, binding to ras, was associated with dynamin II in NIH3T3 cells. Therefore we have tried to identify the relative expression of dynamin II according to overexpressed ras protein in ras oncogene transfected cells (NIH3T3 (ras)). For the detection of differential expression of dynamin II, we have used immunofluorescent staining and western blot methods in NIH3T3 and NIH3T3 (ras) cells. Next we have described the morphological differences between NIH3T3 and NIH3T3 (ras) cells using SEM and TEM. From these experiments dynamin II was highly expressed in NIH3T3 (ras) cells. NIH3T3 cells was transformed to more spindle shape with many cell process by transfection of ras oncogene. Moreover dynamin II was more concentrated in endocytotic membrane of the NIH3T3 (ras) cells compared to that of NIH3T3 cells. The present results suggested that dynamin II may involve the intermediate messenger in Ras signaling transduction pathway.

Expression of Dynamin II in Ameloblast during Mouse Tooth Development (생쥐 치아 발생과정 중 법랑질모세포에서 Dynamin II 발현)

  • Choi, Jung-Mi;Moon, Deog-Hwan;Lee, Jung-Hwa
    • Journal of dental hygiene science
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    • v.12 no.5
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    • pp.486-492
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    • 2012
  • Immunostaing intensity of Dynamin II protein in ameloblast during mouse tooth development showed a significant increase of 48% at the postnatal day 3 and a significant increase of 50% at the postnatal day 5 as compared with the postnatal day 1, but showed a significant decrease of 16% at the postnatal day 7 and a significant decrease of 12% at the postnatal day 10 as compared with the postnatal day 1. From the above results, Dynamin II had relevance to secretion of amelogenin, ameloblastin, enamelin and matrix metalloproteinase-20 proteins for enamel formation in ameloblast. Dynamin II may be involved in the transport of vesicles containing proteins for enamel formation through the acceleration of vesicular formation and may be had a good possibility of secretory regulation of proteins for enamel formation in ameloblast. Therefore, Dynamin II have potential for being used in the field of gene theraphy for periodontal disease and in the regeneration for enamel and dentin tissues lost to dental caries.

Dynamin 2-mediated endocytosis of BLT1 is required for IL-8 production in HMC-1 cells induced by Trichomonas vaginalis-derived secretory products

  • Young Ah Lee;Myeong Heon Shin
    • Parasites, Hosts and Diseases
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    • v.62 no.3
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    • pp.281-293
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    • 2024
  • We previously reported that leukotriene B4 (LTB4) contained in Trichomonas vaginalis-derived secretory products (TvSP) play an essential role in interleukin-8 (IL-8) production in human mast cell line (HMC-1 cells) via LTB4 receptor (BLT)-mediated Nuclear Factor-kappa B (NF-κB) activation. Dynamin, a GTPase, has been known to be involved in endocytosis of receptors for signaling of production of cytokine or chemokines. In the present study, we investigated the role of dynamin-mediated BLT1 endocytosis in TvSP-induced IL-8 production. When HMC-1 cells were transfected with BLT1 or BLT2 siRNA, TvSP-induced IL-8 production was significantly inhibited compared with that in cells transfected with control siRNA. In addition, pretreatment of HMC-1 cells with a dynamin inhibitor (Dynasore) reduced IL-8 production induced by TvSP or LTB4. TvSP- or LTB4-induced phosphorylation of NF-κB was also attenuated by pretreatment with Dynasore. After exposing HMC-1 cells to TvSP or LTB4, BLT1 was translocated from the intracellular compartments to the plasma membrane within 30 min. At 60 min after stimulation with TvSP or LTB4, BLT1 remigrated from the cell surface to intracellular areas. Pretreatment of HMC-1 cells with dynamin-2 siRNA blocked internalization of BLT1 induced by TvSP or LTB4. Co-immunoprecipitation experiments revealed that dynamin-2 strongly interacted with BLT1 60 min after stimulation with TvSP or LTB4. These results suggest that T. vaginalis-secreted LTB4 induces IL-8 production in HMC-1 cells via dynamin 2-mediated endocytosis of BLT1 and phosphorylation of NF-κB.

A family with dynamin 2-related centronuclear myopathy without ocular involvement

  • Park, Jin-Sung;Kim, Dae-Seong;Shin, Jin-Hong
    • Journal of Genetic Medicine
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    • v.13 no.1
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    • pp.51-54
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    • 2016
  • Centronuclear myopathy (CNM) is a rare congenital myopathy that is pathologically characterized by the centrally located nuclei in most of the muscle fibers. On clinical examination, dynamin 2 (DNM2)-related CNM typically shows distal dominant muscle atrophy, ptosis, ophthalmoplegia, and contracture. The reported cases of CNM in Caucasian studies show a high prevalence rate of early-onset ptosis and ophthalmoplegia and correlated with the severity of the disease. However, Asian reports show a low prevalence and late-onset ocular symptoms in DNM2-related CNM patients. p.R465W is one of the most commonly found mutations in Western countries, and all the cases showed ocular symptoms. The proband and his daughter had no ocular symptoms despite harboring the same p.R465W mutation. This family makes us speculate that ocular symptoms in DNM2-related CNM are influenced by ethnic background. In addition, this is the first familial case of DNM2-related CNM in Korea.

Perspective on the Role of Mitochondrial Dynamics in the Nervous System Development (미토콘드리아의 구조적 역동성의 신경계 발생 과정 기능 고찰)

  • Cho, Bong-Ki;Sun, Woong
    • Development and Reproduction
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    • v.13 no.1
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    • pp.13-23
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    • 2009
  • Recent advances in cell biological and genetic researches have revealed that mitochondrial morphology is highly dynamic and regulated by multiple molecular factors including dynamin-related proteins (DRPs). Considering that the mitochondria play critical roles in the cellular metabolism via ATP synthesis, calcium homeostasis in cooperation with endoplasmic reticulum, and apoptosis, the failure of mitochondrial dynamics is infrequently related to the failure in the normal growth and cellular integrity. In this respect, alteration of mitochondrial dynamics may greatly affect the development of nervous system. In this short review, we discussed molecules involved in the control of mitochondrial dynamics, and provide some perspectives on their significance in the neuronal development.

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CoMIC, the hidden dynamics of mitochondrial inner compartments

  • Cho, Bongki;Sun, Woong
    • BMB Reports
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    • v.50 no.12
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    • pp.597-598
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    • 2017
  • Mitochondria have evolutionarily, functionally and structurally distinct outer- (OMM) and inner-membranes (IMM). Thus, mitochondrial morphology is controlled by independent but coordinated activity of fission and fusion of the OMM and IMM. Constriction and division of the OMM are mediated by endocytosis-like machineries, which include dynamin-related protein 1 with additional cytosolic vesicle scissoring machineries such as actin filament and Dynamin 2. However, structural alteration of the IMM during mitochondrial division has been poorly understood. Recently, we found that the IMM and the inner compartments undergo transient and reversible constriction prior to the OMM division, which we termed CoMIC, ${\underline{C}}onstriction$ ${\underline{o}}f$ ${\underline{M}}itochondrial$ ${\underline{I}}nner$ ${\underline{C}}ompartment$. In this short review, we further discuss the evolutionary perspective and the regulatory mechanism of CoMIC during mitochondrial division.

A WD40 Repeat Protein, Arabidopsis Sec13 Homolog 1, May Play a Role in Vacuolar Trafficking by Controlling the Membrane Association of AtDRP2A

  • Lee, Myoung Hui;Lee, Sung Hoon;Kim, Heyran;Jin, Jing Bo;Kim, Dae Heon;Hwang, Inhwan
    • Molecules and Cells
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    • v.22 no.2
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    • pp.210-219
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    • 2006
  • Dynamin-related protein 2A (AtDRP2A, formally ADL6), a member of the dynamin family, is critical for protein trafficking from the TGN to the central vacuole. However, the mechanism controlling its activity is not well understood in plant cells. We isolated Arabidopsis sec13 homolog1 (AtSeh1) that interacts with AtDRP2A by a yeast two-hybrid screening. AtSeh1 has four WD40 motifs and amino acid sequence homology to Sec13, a component of COPII vesicles. Coimmunoprecipitation and protein pull-down experiments demonstrated specific interaction between AtSeh1 and AtDRP2A. AtSeh1 bound to the pleckstrin homology domain of AtDRP2A in competition with the C-terminal domain of the latter, and this resulted in inhibition of the interaction between AtDRP2A and PtdIns3P in vitro. AtSeh1 localized to multiple locations: the nucleus, the prevacuolar compartment and the Golgi complex. Based on these results we propose that AtSeh1 plays a role in regulating cycling of AtDRP2A between membrane-bound and soluble forms.