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Isoform‐Specific Regulation of Na + ,K + ‐ATPase Endocytosis and Recruitment to the Plasma Membrane
Author(s) -
TEIXEIRA VERA LUCAS,
KATZ ADRIAN I.,
PEDEMONTE CARLOS H.,
BERTORELLO ALEJANDRO M.
Publication year - 2003
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2003.tb07257.x
Subject(s) - endocytosis , endosome , intracellular , gene isoform , microbiology and biotechnology , atpase , membrane , chemistry , protein subunit , exocytosis , receptor , biology , biochemistry , enzyme , gene
A bstract : The Na + ,K + ‐ATPase traffics between the plasma membrane and intracellular compartments in response to acute changes in membrane receptor activation. These effects are accomplished by a time‐dependent interaction of the Na + ,K + ‐ATPase α‐subunit with specific intracellular signaling molecules either at the plasma membrane (endocytosis) or at the endosome's membranes (recruitment). Most of these studies have been performed in rat renal epithelial cells in which only the α 1 isoenzyme is present. Studies in neurons from the neostriatum in which all three α‐subunit isoforms are present indicate that neurotransmitter‐dependent regulation of Na + ,K + ‐ATPase activity displays isoform specificity and also suggest a more complex organization of the intracellular signaling networks controlling Na + ,K + ‐ATPase traffic in mammalian cells.