3 datasets found
  1. e

    Q8TAV4

    • ebi.ac.uk
    Updated Aug 29, 2018
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    (2018). Q8TAV4 [Dataset]. https://www.ebi.ac.uk/interpro/protein/Q8TAV4
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    Dataset updated
    Aug 29, 2018
    License

    Attribution 4.0 (CC BY 4.0)https://creativecommons.org/licenses/by/4.0/
    License information was derived automatically

    Description

    Required for the function of many mechanoreceptors. Modulate mechanotransduction channels and acid-sensing ion channels (ASIC) proteins. Potentiates PIEZO1 and PIEZO2 function by increasing their sensitivity to mechanical stimulations

  2. t

    BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on...

    • thebiogrid.org
    zip
    Updated Mar 4, 2013
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    BioGRID Project (2013). BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. [Dataset]. https://thebiogrid.org/151657/publication/cellular-mechanotransduction-relies-on-tension-induced-and-chaperone-assisted-autophagy.html
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    zipAvailable download formats
    Dataset updated
    Mar 4, 2013
    Dataset authored and provided by
    BioGRID Project
    License

    MIT Licensehttps://opensource.org/licenses/MIT
    License information was derived automatically

    Description

    Protein-Protein, Genetic, and Chemical Interactions for Ulbricht A (2013):Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. curated by BioGRID (https://thebiogrid.org); ABSTRACT: Mechanical tension is an ever-present physiological stimulus essential for the development and homeostasis of locomotory, cardiovascular, respiratory, and urogenital systems [1, 2]. Tension sensing contributes to stem cell differentiation, immune cell recruitment, and tumorigenesis [3, 4]. Yet, how mechanical signals are transduced inside cells remains poorly understood. Here, we identify chaperone-assisted selective autophagy (CASA) as a tension-induced autophagy pathway essential for mechanotransduction in muscle and immune cells. The CASA complex, comprised of the molecular chaperones Hsc70 and HspB8 and the cochaperone BAG3, senses the mechanical unfolding of the actin-crosslinking protein filamin. Together with the chaperone-associated ubiquitin ligase CHIP, the complex initiates the ubiquitin-dependent autophagic sorting of damaged filamin to lysosomes for degradation. Autophagosome formation during CASA depends on an interaction of BAG3 with synaptopodin-2 (SYNPO2). This interaction is mediated by the BAG3 WW domain and facilitates cooperation with an autophagosome membrane fusion complex. BAG3 also utilizes its WW domain to engage in YAP/TAZ signaling. Via this pathway, BAG3 stimulates filamin transcription to maintain actin anchoring and crosslinking under mechanical tension. By integrating tension sensing, autophagosome formation, and transcription regulation during mechanotransduction, the CASA machinery ensures tissue homeostasis and regulates fundamental cellular processes such as adhesion, migration, and proliferation.

  3. f

    Vinculin association with actin cytoskeleton is necessary for...

    • plos.figshare.com
    pdf
    Updated Jun 3, 2023
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    Tomohiro Omachi; Takafumi Ichikawa; Yasuhisa Kimura; Kazumitsu Ueda; Noriyuki Kioka (2023). Vinculin association with actin cytoskeleton is necessary for stiffness-dependent regulation of vinculin behavior [Dataset]. http://doi.org/10.1371/journal.pone.0175324
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    pdfAvailable download formats
    Dataset updated
    Jun 3, 2023
    Dataset provided by
    PLOS ONE
    Authors
    Tomohiro Omachi; Takafumi Ichikawa; Yasuhisa Kimura; Kazumitsu Ueda; Noriyuki Kioka
    License

    Attribution 4.0 (CC BY 4.0)https://creativecommons.org/licenses/by/4.0/
    License information was derived automatically

    Description

    The extracellular matrix (ECM) is a major regulator of cell behavior. Recent studies have indicated the importance of the physical properties of the ECM, including its stiffness, for cell migration and differentiation. Using actomyosin-generated forces, cells pull the ECM and sense stiffness via cell-ECM adhesion structures called focal adhesions (FAs). Vinculin, an actin-binding FA protein, has emerged as a major player in FA-mediated mechanotransduction. Although vinculin is important for sensing ECM stiffness, the role of vinculin binding to actin in the ECM stiffness-mediated regulation of vinculin behavior remains unknown. Here, we show that an actin binding-deficient mutation disrupts the ECM stiffness-dependent regulation of CSB (cytoskeleton stabilization buffer) resistance and the stable localization of vinculin. These results suggest that the vinculin-actin interaction participates in FA-mediated mechanotransduction.

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Share
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Click to copy link
Link copied
Close
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BioGRID Project (2013). BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. [Dataset]. https://thebiogrid.org/151657/publication/cellular-mechanotransduction-relies-on-tension-induced-and-chaperone-assisted-autophagy.html

BIOGRID CURATED DATA FOR PUBLICATION: Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy.

Related Article
Explore at:
zipAvailable download formats
Dataset updated
Mar 4, 2013
Dataset authored and provided by
BioGRID Project
License

MIT Licensehttps://opensource.org/licenses/MIT
License information was derived automatically

Description

Protein-Protein, Genetic, and Chemical Interactions for Ulbricht A (2013):Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy. curated by BioGRID (https://thebiogrid.org); ABSTRACT: Mechanical tension is an ever-present physiological stimulus essential for the development and homeostasis of locomotory, cardiovascular, respiratory, and urogenital systems [1, 2]. Tension sensing contributes to stem cell differentiation, immune cell recruitment, and tumorigenesis [3, 4]. Yet, how mechanical signals are transduced inside cells remains poorly understood. Here, we identify chaperone-assisted selective autophagy (CASA) as a tension-induced autophagy pathway essential for mechanotransduction in muscle and immune cells. The CASA complex, comprised of the molecular chaperones Hsc70 and HspB8 and the cochaperone BAG3, senses the mechanical unfolding of the actin-crosslinking protein filamin. Together with the chaperone-associated ubiquitin ligase CHIP, the complex initiates the ubiquitin-dependent autophagic sorting of damaged filamin to lysosomes for degradation. Autophagosome formation during CASA depends on an interaction of BAG3 with synaptopodin-2 (SYNPO2). This interaction is mediated by the BAG3 WW domain and facilitates cooperation with an autophagosome membrane fusion complex. BAG3 also utilizes its WW domain to engage in YAP/TAZ signaling. Via this pathway, BAG3 stimulates filamin transcription to maintain actin anchoring and crosslinking under mechanical tension. By integrating tension sensing, autophagosome formation, and transcription regulation during mechanotransduction, the CASA machinery ensures tissue homeostasis and regulates fundamental cellular processes such as adhesion, migration, and proliferation.

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