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1-6 of 6
Richard I. Morimoto
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Journal Articles
Yo-hei Yamamoto, Ayano Kasai, Hiroko Omori, Tomoe Takino, Munechika Sugihara, Tetsuo Umemoto, Maho Hamasaki, Tomohisa Hatta, Tohru Natsume, Richard I. Morimoto, Ritsuko Arai, Satoshi Waguri, Miyuki Sato, Ken Sato, Shoshana Bar-Nun, Tamotsu Yoshimori, Takeshi Noda, Kazuhiro Nagata
Journal:
Journal of Cell Biology
Journal of Cell Biology (2020) 219 (8): e20190312709142020c.
Published: 23 September 2020
Journal Articles
Yo-hei Yamamoto, Ayano Kasai, Hiroko Omori, Tomoe Takino, Munechika Sugihara, Tetsuo Umemoto, Maho Hamasaki, Tomohisa Hatta, Tohru Natsume, Richard I. Morimoto, Ritsuko Arai, Satoshi Waguri, Miyuki Sato, Ken Sato, Shoshana Bar-Nun, Tamotsu Yoshimori, Takeshi Noda, Kazuhiro Nagata
Journal:
Journal of Cell Biology
Journal of Cell Biology (2020) 219 (8): e201903127.
Published: 03 June 2020
Abstract
In macroautophagy, membrane structures called autophagosomes engulf substrates and deliver them for lysosomal degradation. Autophagosomes enwrap a variety of targets with diverse sizes, from portions of cytosol to larger organelles. However, the mechanism by which autophagosome size is controlled remains elusive. We characterized a novel ER membrane protein, ERdj8, in mammalian cells. ERdj8 localizes to a meshwork-like ER subdomain along with phosphatidylinositol synthase (PIS) and autophagy-related (Atg) proteins. ERdj8 overexpression extended the size of the autophagosome through its DnaJ and TRX domains. ERdj8 ablation resulted in a defect in engulfing larger targets. C. elegans , in which the ERdj8 orthologue dnj-8 was knocked down, could perform autophagy on smaller mitochondria derived from the paternal lineage but not the somatic mitochondria. Thus, ERdj8 may play a critical role in autophagosome formation by providing the capacity to target substrates of diverse sizes for degradation.
Journal Articles
In Special Collection:
Cellular Mechanisms of Aging
Journal:
Journal of Cell Biology
Journal of Cell Biology (2017) 216 (5): 1231–1241.
Published: 11 April 2017
Abstract
The proteostasis network (PN) regulates protein synthesis, folding, transport, and degradation to maintain proteome integrity and limit the accumulation of protein aggregates, a hallmark of aging and degenerative diseases. In multicellular organisms, the PN is regulated at the cellular, tissue, and systemic level to ensure organismal health and longevity. Here we review these three layers of PN regulation and examine how they collectively maintain cellular homeostasis, achieve cell type-specific proteomes, and coordinate proteostasis across tissues. A precise understanding of these layers of control has important implications for organismal health and could offer new therapeutic approaches for neurodegenerative diseases and other chronic disorders related to PN dysfunction.
Journal Articles
Journal:
Journal of Cell Biology
Journal of Cell Biology (2005) 171 (1): 75–85.
Published: 10 October 2005
Abstract
The appearance of protein aggregates is a characteristic of protein misfolding disorders including familial amyotrophic lateral sclerosis, a neurodegenerative disease caused by inherited mutations in Cu/Zn superoxide dismutase 1 (SOD1). Here, we use live cell imaging of neuronal and nonneuronal cells to show that SOD1 mutants (G85R and G93A) form an aggregate structure consisting of immobile scaffolds, through which noninteracting cellular proteins can diffuse. Hsp70 transiently interacts, in a chaperone activity-dependent manner, with these mutant SOD1 aggregate structures. In contrast, the proteasome is sequestered within the aggregate structure, an event associated with decreased degradation of a proteasomal substrate. Through the use of time-lapse microscopy of individual cells, we show that nearly all (90%) aggregate-containing cells express higher levels of mutant SOD1 and died within 48 h, whereas 70% of cells expressing a soluble mutant SOD1 survived. Our results demonstrate that SOD1 G85R and G93A mutants form a distinct class of aggregate structures in cells destined for neuronal cell death.
Includes: Supplementary data
Journal Articles
Caroline Jolly, Lara Konecny, Deborah L. Grady, Yulia A. Kutskova, José J. Cotto, Richard I. Morimoto, Claire Vourc'h
Journal:
Journal of Cell Biology
Journal of Cell Biology (2002) 156 (5): 775–781.
Published: 04 March 2002
Abstract
Activation of the mammalian heat shock transcription factor (HSF)1 by stress is a multistep process resulting in the transcription of heat shock genes. Coincident with these events is the rapid and reversible redistribution of HSF1 to discrete nuclear structures termed HSF1 granules, whose function is still unknown. Key features are that the number of granules correlates with cell ploidy, suggesting the existence of a chromosomal target. Here we show that in humans, HSF1 granules localize to the 9q11-q12 heterochromatic region. Within this locus, HSF1 binds through direct DNA–protein interaction with a nucleosome-containing subclass of satellite III repeats. HSF1 granule formation only requires the DNA binding competence and the trimerization of the factor. This is the first example of a transcriptional activator that accumulates transiently and reversibly on a chromosome-specific heterochromatic locus.
Journal Articles
Journal:
Journal of Cell Biology
Journal of Cell Biology (1999) 145 (6): 1133–1143.
Published: 14 June 1999
Abstract
The cell nucleus is organized as discrete domains, often associated with specific events involved in chromosome organization, replication, and gene expression. We have examined the spatial and functional relationship between the sites of heat shock gene transcription and the speckles enriched in splicing factors in primary human fibroblasts by combining immunofluorescence and fluorescence in situ hybridization (FISH). The hsp90α and hsp70 genes are inducibly regulated by exposure to stress from a low basal level to a high rate of transcription; additionally the hsp90α gene contains 10 introns whereas the hsp70 gene is intronless. At 37°C, only 30% of hsp90α transcription sites are associated with speckles whereas little association is detected with the hsp70 gene, whose constitutive expression is undetectable relative to the hsp90α gene. Upon exposure of cells to heat shock, the heavy metal cadmium, or the amino acid analogue azetidine, transcription at the hsp90α and hsp70 gene loci is strongly induced, and both hsp transcription sites become associated with speckles in >90% of the cells. These results reveal a clear disconnection between the presence of intervening sequences at specific gene loci and the association with splicing factor–rich regions and suggest that subnuclear structures containing splicing factors are associated with sites of transcription.