TY - JOUR
T1 - Role of kinesin light chain-2 of kinesin-1 in the traffic of Na,K-ATPase-containing vesicles in alveolar epithelial cells
AU - Trejo, Humberto E.
AU - Lecuona, Emilia
AU - Grillo, Doris
AU - Szleifer, Igal
AU - Nekrasova, Oksana E.
AU - Gelfand, Vladimir I.
AU - Sznajder, Jacob I.
PY - 2010/2
Y1 - 2010/2
N2 - 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. Knock-down 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.
AB - 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. Knock-down 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.
KW - Intracellular traffic
KW - Molecular motors
KW - Sodium pump
UR - http://www.scopus.com/inward/record.url?scp=76149115569&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=76149115569&partnerID=8YFLogxK
U2 - 10.1096/fj.09-137802
DO - 10.1096/fj.09-137802
M3 - Article
C2 - 19773350
AN - SCOPUS:76149115569
SN - 0892-6638
VL - 24
SP - 374
EP - 382
JO - FASEB Journal
JF - FASEB Journal
IS - 2
ER -