TITLE

The role of actin remodeling in the trafficking of intracellular vesicles, transporters, and channels: focusing on aquaporin-2

AUTHOR(S)
Noda, Yumi; Sasaki, Sei
PUB. DATE
July 2008
SOURCE
Pflugers Archiv European Journal of Physiology;Jul2008, Vol. 456 Issue 4, p737
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Trafficking of the intracellular vesicles and membrane protein incorporated in the vesicles is essential for a variety of basic biological processes. Growing evidence has highlighted the importance of the actin cytoskeleton in the trafficking of synaptic vesicles, secretory granules, transporters, and channels including aquaporin. These trafficking processes require actin remodeling, which is spatiotemporally regulated. Recent researches have come to focus on the motility mechanism of the translocation. In this review, we describe the role of actin at each step of intracellular reservation, exocytosis, docking, fusion with the plasma membrane, and endocytosis, focusing on aquaporin-2 trafficking.
ACCESSION #
31998989

 

Related Articles

  • Real-Time Measurement of F-Actin Remodelling during Exocytosis Using Lifeact-EGFP Transgenic Animals. Yujin Jang; Soekmadji, Carolina; Mitchell, Justin M.; Thomas, Walter G.; Thorn, Peter // PLoS ONE;Jul2012, Vol. 7 Issue 7, p1 

    F-actin remodelling is essential for a wide variety of cell processes. It is important in exocytosis, where F-actin coats fusing exocytic granules. The purpose of these F-actin coats is unknown. They may be important in stabilizing the fused granules, they may play a contractile role and promote...

  • Ca2+-induced exocytosis in individual human neutrophils: high- and low-affinity granule populations and submaximal responses. Nüße, Oliver; Serrander, Lena; Lew, Daniel P.; Krause, Karl-Heinz // EMBO Journal;3/1/98, Vol. 17 Issue 5, p1279 

    We have investigated Ca2+-induced exocytosis from human neutrophils using the whole cell patch­clamp capacitance technique. Microperfusion of Ca2+ buffer solutions (<30 nM to 5 mM free Ca2+) through the patch­clamp pipette revealed a biphasic activation of exocytosis by Ca2+. The first...

  • aquaporin.  // Taber's Cyclopedic Medical Dictionary (2009);2009, Issue 21, p170 

    A definition of the term "aquaporin," which pertains to a cell membrane protein that lets water flow into and out of cells, is presented.

  • a-latrotoxin triggers transmitter release via direct insertion into the presynaptic plasma membrane. Khvotchev, Mikhail; Südhof, Thomas C. // EMBO Journal;7/1/2000, Vol. 19 Issue 13, p3250 

    &alpha-latrotoxin, a component of black widow spider venom, binds to presynaptic nerve terminals and stimulates massive neucotransmitter release. Previous studies have demonstrated that α-latrotoxin first binds to two high-affinity receptors on nerve terminals, neurexins and CLs (CIRLs and...

  • Introduction for Special issue for Aquaporin. Sasaki, Sei // Pflugers Archiv European Journal of Physiology;Jul2008, Vol. 456 Issue 4, p647 

    The article discusses various reports published within the issue including one by Richard K. Hite, Tamir Gonen and Stephen C. Harrison on the cell membranes and lipids with aquaporin interactions, another one by Tomayo Nishimo and Oliver Devuyst on clinical applications on the research regarding...

  • Proteomic analysis of secretagogue-stimulated neutrophils implicates a role for actin and actin-interacting proteins in Rac2-mediated granule exocytosis.  // Proteome Science;2011 Supplement 1, Vol. 9 Issue Suppl 1, p70 

    The article presents the findings of a research conducted for identifying Rho GTPases, particularly Rac2-dependent changes in protein abundance in stimulated neutrophils. Under the research, proteomic analysis on secretagogue-stimulated bone marrow neutrophils was performed, which represented a...

  • Neurexin mediates the assembly of presynaptic terminals. Dean, Camin; Scholl, Francisco G; Choih, Jenny; DeMaria, Shannon; Berger, James; Isacoff, Ehud; Scheiffele, Peter // Nature Neuroscience;Jul2003, Vol. 6 Issue 7, p708 

    Neurexins are a large family of proteins that act as neuronal cell-surface receptors. The function and localization of the various neurexins, however, have not yet been clarified. Beta-neurexins are candidate receptors for neuroligin-1, a postsynaptic membrane protein that can trigger synapse...

  • From structure to disease: the evolving tale of aquaporin biology. King, Landon S.; Kozono, David; Agre, Peter // Nature Reviews Molecular Cell Biology;Sep2004, Vol. 5 Issue 9, p687 

    Our understanding of the movement of water through cell membranes has been greatly advanced by the discovery of a family of water-specific, membrane-channel proteins-the aquaporins. These proteins are present in organisms at all levels of life, and their unique permeability characteristics and...

  • Loop A Is Critical for the Functional Interaction of Two Beta vulgaris PIP Aquaporins. Jozefkowicz, Cintia; Rosi, Pablo; Sigaut, Lorena; Soto, Gabriela; Pietrasanta, Lía Isabel; Amodeo, Gabriela; Alleva, Karina // PLoS ONE;Mar2013, Vol. 8 Issue 3, p1 

    Research done in the last years strongly support the hypothesis that PIP aquaporin can form heterooligomeric assemblies, specially combining PIP2 monomers with PIP1 monomers. Nevertheless, the structural elements involved in the ruling of homo versus heterooligomeric organization are not...

Share

Read the Article

Courtesy of THE LIBRARY OF VIRGINIA

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics