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Role of kinesin light chain‐2 of kinesin‐1 in the traffic of Na,K‐ATPase‐containing vesicles in alveolar epithelial cells
Author(s) -
Trejo Humberto E.,
Lecuona Emilia,
Grillo Doris,
Szleifer Igal,
Nekrasova Oksana E.,
Gelfand Vladimir I.,
Sznajder Jacob I.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.09-137802
Subject(s) - kinesin , microtubule , microbiology and biotechnology , vesicle , chemistry , atpase , organelle , v atpase , dynein , immunoglobulin light chain , motor protein , biophysics , biology , biochemistry , membrane , enzyme , immunology , antibody
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 the light chain‐1 (KLC1), decreased the 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—Trejo, H. E., Lecuona, E., Grillo, D., Szleifer, I., Nekrasova, O. E., Gelfand, V. I., Sznajder, J. I. Role of kinesin light chain‐2 of kinesin‐1 in the traffic of Na,K‐ATPase‐containing vesicles in alveolar epithelial cells. FASEB J . 24, 374–382 (2010). www.fasebj.org