Myosin-Va restrains the trafficking of Na+/K+-ATPase-containing vesicles in alveolar epithelial cells
| Autor: | Doris Grillo, Haiying Sun, Igal Szleifer, Oxana Nekrasova, Jiwang Chen, Emilia Lecuona, Humberto E. Trejo, Jacob I. Sznajder, Vladimir I. Gelfand, Lynn C. Welch, Alexander A. Minin, Alejandro P. Comellas |
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| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Sodium-Potassium-Exchanging ATPase
Myosin Type V Biology Cell Line Cell membrane Myosin medicine Cyclic AMP Animals Humans Protein Isoforms Na+/K+-ATPase Actin Myosin Heavy Chains Vesicle Cell Membrane Cytoplasmic Vesicles Epithelial Cells Cell Biology Transport protein Cell biology Rats Pulmonary Alveoli Protein Transport medicine.anatomical_structure Intracellular Research Article |
| Popis: | Stimulation of Na(+)/K(+)-ATPase activity in alveolar epithelial cells by cAMP involves its recruitment from intracellular compartments to the plasma membrane. Here, we studied the role of the actin molecular motor myosin-V in this process. We provide evidence that, in alveolar epithelial cells, cAMP promotes Na(+)/K(+)-ATPase recruitment to the plasma membrane by increasing the average speed of Na(+)/K(+)-ATPase-containing vesicles moving to the cell periphery. We found that three isoforms of myosin-V are expressed in alveolar epithelial cells; however, only myosin-Va and Vc colocalized with the Na(+)/K(+)-ATPase in intracellular membrane fractions. Overexpression of dominant-negative myosin-Va or knockdown with specific shRNA increased the average speed and distance traveled by the Na(+)/K(+)-ATPase-containing vesicles, as well as the Na(+)/K(+)-ATPase activity and protein abundance at the plasma membrane to similar levels as those observed with cAMP stimulation. These data show that myosin-Va has a role in restraining Na(+)/K(+)-ATPase-containing vesicles within intracellular pools and that this restrain is released after stimulation by cAMP allowing the recruitment of the Na(+)/K(+)-ATPase to the plasma membrane and thus increased activity. |
| Databáze: | OpenAIRE |
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