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JUNQ and IPOD are types of cytosolic protein inclusion bodies in eukaryotes. Neurodegenerative diseases, such as Parkinson's, Alzheimer's, and Huntington's, are associated and correlated with protein aggregation and accumulation of misfolded proteins in inclusion bodies. For many years, protein aggregation was considered a random process by which misfolded proteins stick to each other to form inclusions (imagine a bundle of hairs haphazardly piling up in a corner of a room). Moreover, protein aggregates were thought to be toxic agents and the cause for neuronal dysfunction and death. However, recent studies, using advanced methods (i.e. fluorescence microscopy), show that protein aggregation may actually be a tightly regulated, organized process, by which the cell protects itself from toxi

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  • JUNQ and IPOD (en)
  • JUNQ et IPOD (fr)
  • JUNQとIPOD (ja)
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  • JUNQ and IPOD are types of cytosolic protein inclusion bodies in eukaryotes. Neurodegenerative diseases, such as Parkinson's, Alzheimer's, and Huntington's, are associated and correlated with protein aggregation and accumulation of misfolded proteins in inclusion bodies. For many years, protein aggregation was considered a random process by which misfolded proteins stick to each other to form inclusions (imagine a bundle of hairs haphazardly piling up in a corner of a room). Moreover, protein aggregates were thought to be toxic agents and the cause for neuronal dysfunction and death. However, recent studies, using advanced methods (i.e. fluorescence microscopy), show that protein aggregation may actually be a tightly regulated, organized process, by which the cell protects itself from toxi (en)
  • Les JUNQ et IPOD constituent des types de structures d'inclusion de protéines cytosoliques qu'on retrouve chez les eucaryotes. Des maladies neurodégénératives, comme celles de Parkinson, Alzheimer et Huntington, sont associées et corrélées à l'agrégation des protéines et l'accumulation de protéines mal repliées dans ces structures d'inclusion. Pendant de nombreuses années, l'agrégation protéique était considérée comme un processus aléatoire par lequel les protéines mal repliées se collent entre elles pour former des inclusions (s'imaginer un paquet de cheveux qui s'empilent de façon désordonnée dans le coin d'une pièce). De plus, on pensait que les agrégats protéiques étaient des agents toxiques ainsi que la cause d'un dysfonctionnement neuronal pouvant conduire à la mort. Cependant, des é (fr)
  • JUNQとIPODは、真核生物の細胞質に見られるタンパク質の封入体である。 パーキンソン病、アルツハイマー病、ハンチントン病などの疾患は神経変性疾患と総称され、タンパク質凝集やミスフォールドタンパク質の封入体への蓄積を伴う。かつてよりタンパク質の凝集は、ミスフォールドしたタンパク質がお互いに結合して封入体を形成するランダムな過程と考えられてきた。また、タンパク質の凝集体は毒性を持つ物質として、神経細胞の機能障害や細胞死を引き起こすものと考えられてきた。しかし近年、蛍光顕微鏡などの先端技術を用いた研究により、タンパク質凝集という現象は実際には厳密に制御されたプロセスであること、そして細胞は毒性タンパク質を封入体に隔離することで、自らを保護していることが明らかとなった。2008年、ダニエル・カガノヴィッチは、真核細胞はその巧妙に管理された細胞プロセスにより、ミスフォールドしたタンパク質を(以下に列挙する)2種類の封入体へ仕分けをしていることを示した。 1. * JUNQ(JUxta Nuclear Quality control compartment、意味:核近傍品質管理コンパートメント) 2. * IPOD(Insoluble Protein Deposit、意味:不溶性タンパク質保管所) (ja)
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  • http://commons.wikimedia.org/wiki/Special:FilePath/A_scheme_of_a_yeast_cell_harboring_JUNQ_and_IPOD_inclusions.png
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