A5012863354- Barrier Structure and Function Studies
- Connexins and lens biology
- Endoplasmic Reticulum Stress and Disease
- Caveolin-1 and cellular processes
- Microtubule and mitosis dynamics
- Phagocytosis and Immune Regulation
- Autophagy in Disease and Therapy
- Extracellular vesicles in disease
- Immunotherapy and Immune Responses
- Neurological Disease Mechanisms and Treatments
- Cancer Immunotherapy and Biomarkers
- Ubiquitin and proteasome pathways
- Ion Channels and Receptors
- RNA Interference and Gene Delivery
- Pediatric health and respiratory diseases
- Cancer-related molecular mechanisms research
- Transgenic Plants and Applications
- Image Processing Techniques and Applications
- Neurological diseases and metabolism
- Hearing, Cochlea, Tinnitus, Genetics
- Neonatal skin health care
- Cancer Cells and Metastasis
- Plant Reproductive Biology
- Hippo pathway signaling and YAP/TAZ
- Cellular transport and secretion
Kyoto University
2003-2023
Kobe University
2009-2020
Institute of Cell Biology
2014
Teikyo University
2011
Japan Science and Technology Agency
2007
Frontier Medical College
2006
Foundation for Applied Molecular Evolution
2006
Terminally misfolded proteins in the endoplasmic reticulum (ER) are retrotranslocated to cytoplasm and degraded by proteasomes through a mechanism known as ER-associated degradation (ERAD). EDEM, postulated Man8B-binding protein, accelerates of ER. Here, EDEM was shown interact with calnexin, but not calreticulin, its transmembrane region. Both binding substrates calnexin their release from were required for ERAD occur. Overexpression accelerated promoting terminally calnexin. Thus, appeared...
Proteins that are unfolded or misfolded in the endoplasmic reticulum (ER) must be refolded degraded to maintain homeostasis of ER. Components both productive folding and ER-associated degradation (ERAD) mechanisms known up-regulated by protein response (UPR). We describe two novel components mammalian ERAD, Derlin-2 -3, which show weak homology Der1p, a transmembrane involved yeast ERAD. Both -3 UPR, at least is target IRE1 branch response, up-regulate ER enhancing α-mannosidase–like (EDEM)...
Epithelial cell contacts consist of not only bicellular but also tricellular contacts, where the corners three cells meet. At tight junctions (TJs) generate specialized structures termed TJs (tTJs) to seal intercellular space. Tricellulin is known molecular component tTJs and involved in formation tTJs, as well normal epithelial barrier function. However, detailed mechanism how are formed maintained remains elusive. Using a localization-based expression cloning method, we identified novel...
Misfolded or improperly assembled proteins in the endoplasmic reticulum (ER) are exported into cytosol and degraded via ubiquitin-proteasome pathway, a process termed ER-associated degradation (ERAD). Saccharomyces cerevisiae Hrd1p/Der3p is an ER membrane-spanning ubiquitin ligase that participates ERAD of cystic fibrosis transmembrane conductance regulator (CFTR) when CFTR exogenously expressed yeast cells. Two mammalian orthologues Hrd1p/Der3p, gp78 HRD1, have been reported. Here, we...
Tricellular tight junctions (tTJs) seal the extracellular space at tricellular contacts (TCs), where corners of three epithelial cells meet. To date, transmembrane proteins tricellulin and lipolysis-stimulated lipoprotein receptor (LSR) are known to be molecular components tTJs. LSR recruits tTJs, both required for full barrier function cellular sheets. Here, we show that two LSR-related proteins, immunoglobulin-like domain-containing (ILDR)1 ILDR2, also localized TCs recruit tricellulin....
The structural continuity of tight junctions (TJs) is consistently maintained even when epithelial cells divide and move within the cellular sheet. This process associated with dynamic remodeling TJs by coordinated internalization generation claudin-based TJ strands, but molecular mechanism behind regulated turnover remains largely unknown. In this study, we identified p80 isoform E3 ubiquitin ligase ligand Numb-protein X1 (LNX1p80) as a protein binding to claudin-1. Interestingly,...
There was an error published in J. Cell Sci. 126, 966-977.There are mistakes the notation of a mutant protein. All instances R89Q (including figures) should fact be R97Q.The authors apologise for this mistake.
When the surface view of each epithelial cell is compared with a polygon, its sides correspond to cell–cell junctions, while vertices tricellular contacts, whose roles in morphogenesis have not been well studied. Here, we show that tricellulin, which localized at regulates F-actin organization via Cdc42. Tricellulin knockdown cells exhibit irregular polygonal shapes curved borders and impaired fibers around contacts during junction formation. The N-terminal cytoplasmic domain tricellulin...
Tricellular tight junctions (tTJs) are specialized structural variants of that restrict the free diffusion solutes at extracellular space tricellular contacts. Their presence cell corners, situated in angles between three adjacent epithelial cells, was identified early by electron microscopy, but despite their potential importance, tTJs have been generally ignored biology. Tricellulin first molecular component shown to be involved formation and barrier function. However, precise organization...
Tricellular tight junctions (t TJ s) are specialized structural variants of within tricellular contacts an epithelial sheet and comprise several transmembrane proteins including lipolysis‐stimulated lipoprotein receptor (angulin‐1/LSR) tricellulin. To elucidate the mechanism its formation, we carried out stepwise screening kinase inhibitors followed by RNA i to identify kinases that regulate intracellular localization angulin‐1/ LSR tTJs using a fluorescence image‐based screen. We found...
Tricellular tight junctions (tTJs) create paracellular barriers at tricellular contacts (TCs), where the vertices of three polygonal epithelial cells meet. tTJs are marked by enrichment two types membrane proteins, tricellulin and angulin family proteins. However, how TC geometry is recognized for tTJ formation remains unknown. In present study, we examined molecular mechanism assembly angulin-1 TCs. We found that clusters cysteine residues in juxtamembrane region within cytoplasmic domain...
McKusick-Kaufman syndrome (MKKS) is a recessively inherited human genetic disease characterized by several developmental anomalies. Mutations in the MKKS gene also cause Bardet-Biedl (BBS), genetically heterogeneous disorder with pleiotropic symptoms. However, little known about how mutations lead to disease. Here, we show that disease-causing mutants of are rapidly degraded via ubiquitin-proteasome pathway manner dependent on HSC70 interacting protein (CHIP), chaperone-dependent ubiquitin...
C-terminal alpha 1-antitrypsin peptides induce tight junction formation by activating G protein G13.
Abstract Cell extrusion is a universal mode of cell removal from tissues, and it plays an important role in regulating numbers eliminating unwanted cells, such as apoptotic, unfit, or cancerous. During this process, cells delaminate the layer, however, underlying mechanisms remain to be elucidated. Here, we report conserved execution mechanism extrusion. We found extracellular vesicle (EV) formation extruding at site opposite direction. Particularly, that lipid-scramblase‒mediated local...
Abstract Numerous unwanted cells are removed from epithelial and endothelial tissues—in which tightly connected to one another—without disturbing tissue integrity homeostasis. Cell extrusion is a unique mode of cell removal tissues, it plays an important role in regulating numbers the eliminating cells, such as apoptotic cancer with lower fitness competition . During this process, delaminate layer, they initially used adhere, through communication neighboring cells. Defects believed...