Role of kinesin light chain-2 of kinesin-1 in the traffic of Na,K-ATPase-containing vesicles in alveolar epithelial cells.

Autor: Trejo, Humberto E., Lecuona, Emilia, Grillo, Doris, Szleifer, Igal, Nekrasova, Oksana E., Gelfand, Vladimir I., Sznajder, Jacob I.
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Zdroj: FASEB Journal; Feb2010, Vol. 24 Issue 2, p374-382, 9p, 1 Diagram, 4 Graphs
Abstrakt: Recruitment of the Na,K-ATPase to the plasma membrane of alveolar epithelial cells results in increased active Na+ transport and fluid clearance in a process that requires an intact microtubule network. However, the microtubule motors involved in this process have not been identified. In the present report, we studied the role of kinesin-1, a plus-end microtubule molecular motor that has been implicated in the movement of organelles in the Na,K-ATPase traffic. We determined by confocal microscopy and biochemical assays that kinesin-1 and the Na,K-ATPase are present in the same membranous cellular compartment. Knockdown of kinesin-1 heavy chain (KHC) or the light chain-2 (KLC2), but not of die light chain-1 (KLC1), decreased die movement of Na,K-ATPase-containing vesicles when compared to sham siRNA-transfected cells (control group). Thus, a specific isoform of kinesin-1 is required for microtubule-dependent recruitment of Na,K-ATPase to the plasma membrane, which is of physiological significance. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index