• Login
    About WHOAS
    View Item 
    •   WHOAS Home
    • Marine Biological Laboratory
    • BioCurrents Research Center
    • View Item
    •   WHOAS Home
    • Marine Biological Laboratory
    • BioCurrents Research Center
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of WHOASCommunities & CollectionsBy Issue DateAuthorsTitlesKeywordsThis CollectionBy Issue DateAuthorsTitlesKeywords

    My Account

    LoginRegister

    Statistics

    View Usage Statistics

    Modulation of the actin cytoskeleton via gelsolin regulates aacuolar H+-ATPase recycling

    Thumbnail
    View/Open
    8452.pdf (595.7Kb)
    Date
    2004-12-09
    Author
    Beaulieu, Valerie  Concept link
    Da Silva, Nicolas  Concept link
    Pastor-Soler, Nuria  Concept link
    Brown, Christopher R.  Concept link
    Smith, Peter J. S.  Concept link
    Brown, Dennis  Concept link
    Breton, Sylvie  Concept link
    Metadata
    Show full item record
    Citable URI
    https://hdl.handle.net/1912/2809
    As published
    https://doi.org/10.1074/jbc.M412750200
    DOI
    10.1074/jbc.M412750200
    Abstract
    The role of the actin cytoskeleton in regulating membrane protein trafficking is complex and depends on the cell type and protein being examined. Using the epididymis as a model system in which luminal acidification is crucial for sperm maturation and storage, we now report that modulation of the actin cytoskeleton by the calcium-activated actin-capping and -severing protein gelsolin plays a key role in regulating vacuolar H+-ATPase (V-ATPase) recycling. Epididymal clear cells contain abundant V-ATPase in their apical pole, and an increase in their cell-surface V-ATPase expression correlates with an increase in luminal proton secretion. We have shown that apical membrane accumulation of V-ATPase is triggered by an elevation in cAMP following activation of bicarbonate-regulated soluble adenylyl cyclase in response to alkaline luminal pH (Pastor-Soler, N., Beaulieu, V., Litvin, T. N., Da Silva, N., Chen, Y., Brown, D., Buck, J., Levin, L. R., and Breton, S. (2003) J. Biol. Chem. 278, 49523-49529). Here, we show that clear cells express high levels of gelsolin, indicating a potential role in the functional activity of these cells. When jasplakinolide was used to overcome the severing action of gelsolin by polymerizing actin, complete inhibition of the alkaline pH- and cAMP-induced apical membrane accumulation of V-ATPase was observed. Conversely, when gelsolin-mediated actin filament elongation was inhibited using a 10-residue peptide (PBP10) derived from the phosphatidylinositol 4,5-bisphosphate-binding region (phosphoinositide-binding domain 2) of gelsolin, significant V-ATPase apical membrane mobilization was induced, even at acidic luminal pH. In contrast, the calcium chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetrakis(acetoxymethyl ester) and the phospholipase C inhibitor U-73122 inhibited the alkaline pH-induced V-ATPase apical accumulation. Thus, maintenance of the actin cytoskeleton in a depolymerized state by gelsolin facilitates calcium-dependent apical accumulation of V-ATPase in response to luminal pH alkalinization. Gelsolin is present in other cell types that express the V-ATPase in their plasma membrane and recycling vesicles, including kidney intercalated cells and osteoclasts. Therefore, modulation of the actin cortex by this severing and capping protein may represent a common mechanism by which these cells regulate their rate of proton secretion.
    Description
    Author Posting. © American Society for Biochemistry and Molecular Biology, 2005. This article is posted here by permission of American Society for Biochemistry and Molecular Biology for personal use, not for redistribution. The definitive version was published in Journal of Biological Chemistry 280 (2005): 8452-8463, doi:10.1074/jbc.M412750200.
    Collections
    • BioCurrents Research Center
    Suggested Citation
    Journal of Biological Chemistry 280 (2005): 8452-8463
     

    Related items

    Showing items related by title, author, creator and subject.

    • Thumbnail

      Inhibition of fast axonal transport by pathogenic SOD1 involves activation of p38 MAP kinase 

      Morfini, Gerardo A.; Bosco, Daryl A.; Brown, Hannah; Gatto, Rodolfo; Kaminska, Agnieszka; Song, Yuyu; Molla, Linda; Baker, Lisa; Marangoni, M. Natalia; Berth, Sarah; Tavassoli, Ehsan; Bagnato, Carolina; Tiwari, Ashutosh; Hayward, Lawrence J.; Pigino, Gustavo F.; Watterson, D. Martin; Huang, Chun-Fang; Banker, Gary; Brown, Robert H.; Brady, Scott T. (Public Library of Sceince, 2013-06-12)
      Dying-back degeneration of motor neuron axons represents an established feature of familial amyotrophic lateral sclerosis (FALS) associated with superoxide dismutase 1 (SOD1) mutations, but axon-autonomous effects of ...
    • Thumbnail

      Estimating the recharge properties of the deep ocean using noble gases and helium isotopes 

      Loose, Brice; Jenkins, William J.; Moriarty, Roisin; Brown, Peter; Jullion, Loic; Naveira Garabato, Alberto C.; Valdes, Sinhue Torres; Hoppema, Mario; Ballentine, Chris; Meredith, Michael P. (John Wiley & Sons, 2016-08-18)
      The distribution of noble gases and helium isotopes in the dense shelf waters of Antarctica reflects the boundary conditions near the ocean surface: air-sea exchange, sea ice formation, and subsurface ice melt. We use a ...
    • Thumbnail

      Real-time reporting of baleen whale passive acoustic detections from ocean gliders 

      Baumgartner, Mark F.; Fratantoni, David M.; Hurst, Thomas P.; Brown, Moira W.; Cole, Timothy V. N.; Van Parijs, Sofie M.; Johnson, Mark P. (Acoustical Society of America, 2013-08)
      In the past decade, much progress has been made in real-time passive acoustic monitoring of marine mammal occurrence and distribution from autonomous platforms (e.g., gliders, floats, buoys), but current systems focus ...
    All Items in WHOAS are protected by original copyright, with all rights reserved, unless otherwise indicated. WHOAS also supports the use of the Creative Commons licenses for original content.
    A service of the MBLWHOI Library | About WHOAS
    Contact Us | Send Feedback | Privacy Policy