{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cai T"],"funding":["NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["1153-69"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2542476"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["182(6)"],"pubmed_abstract":["Here, we show that the Na/K-ATPase interacts with caveolin-1 (Cav1) and regulates Cav1 trafficking. Graded knockdown of Na/K-ATPase decreases the plasma membrane pool of Cav1, which results in a significant reduction in the number of caveolae on the cell surface. These effects are independent of the pumping function of Na/K-ATPase, and instead depend on interaction between Na/K-ATPase and Cav1 mediated by an N-terminal caveolin-binding motif within the ATPase alpha1 subunit. Moreover, knockdown of the Na/K-ATPase increases basal levels of active Src and stimulates endocytosis of Cav1 from the plasma membrane. Microtubule-dependent long-range directional trafficking in Na/K-ATPase-depleted cells results in perinuclear accumulation of Cav1-positive vesicles. Finally, Na/K-ATPase knockdown ha"],"journal":["The Journal of cell biology"],"pubmed_title":["Regulation of caveolin-1 membrane trafficking by the Na/K-ATPase."],"pmcid":["PMC2542476"],"funding_grant_id":["P01 HL036573","GM-78565","R01 GM078565","HL-36573","R01 HL067963"],"pubmed_authors":["Cai T","Liu L","Quintas LE","Gunning WT","Chen Y","Wang H","Xie ZJ"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of caveolin-1 membrane trafficking by the Na/K-ATPase.","description":"Here, we show that the Na/K-ATPase interacts with caveolin-1 (Cav1) and regulates Cav1 trafficking. Graded knockdown of Na/K-ATPase decreases the plasma membrane pool of Cav1, which results in a significant reduction in the number of caveolae on the cell surface. These effects are independent of the pumping function of Na/K-ATPase, and instead depend on interaction between Na/K-ATPase and Cav1 mediated by an N-terminal caveolin-binding motif within the ATPase alpha1 subunit. Moreover, knockdown of the Na/K-ATPase increases basal levels of active Src and stimulates endocytosis of Cav1 from the plasma membrane. Microtubule-dependent long-range directional trafficking in Na/K-ATPase-depleted cells results in perinuclear accumulation of Cav1-positive vesicles. Finally, Na/K-ATPase knockdown ha","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Sep","modification":"2025-04-04T13:11:14.395Z","creation":"2019-03-27T00:16:41Z"},"accession":"S-EPMC2542476","cross_references":{"pubmed":["18794328"],"doi":["10.1083/jcb.200712022"]}}