Cys palmitoylation of the β subunit modulates gating of the epithelial sodium channel

Journal of Biological Chemistry

Volumn 285, Issue 40, 2010, Pages 30453-30462

  Mueller, Gunhild M ^a   Maarouf, Ahmad B ^a   Kinlough, Carol L ^a   Sheng, Nan ^a   Kashlan, Ossama B ^a   Okumura, Sora ^a   Luthy, Sarah ^a   Kleyman, Thomas R ^a   Hughey, Rebecca P ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMILORIDE; AMPHIPATHIC; CHANNEL GATING; COMPUTER MODELING; CYS RESIDUES; CYTOPLASMIC DOMAINS; EPITHELIAL SODIUM CHANNELS; EXTRACELLULAR REGION; MEMBRANE TRAFFICKING; PALMITOYLATION; PLASMA MEMBRANES; SECOND TRANSMEMBRANE DOMAIN; SELF-INHIBITION; SINGLE CHANNELS; SURFACE EXPRESSION; TRANS-MEMBRANE DOMAINS; TRANSMEMBRANES; WHOLE CELL; WILD TYPES; XENOPUS OOCYTE;

ACTIVATION ANALYSIS; BIOLOGICAL MEMBRANES; CELL MEMBRANES; FATTY ACIDS;

SODIUM;

CYSTEINE; EPITHELIAL SODIUM CHANNEL; AMILORIDE; SODIUM; SODIUM CHANNEL BLOCKING AGENT;

ALPHA HELIX; ANIMAL CELL; ARTICLE; BETA CHAIN; CELL MEMBRANE; CHANNEL GATING; COMPUTER MODEL; CONTROLLED STUDY; MEMBRANE TRANSPORT; MUTANT; NONHUMAN; OOCYTE; PALMITOYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; WILD TYPE; XENOPUS; AMINO ACID SUBSTITUTION; ANIMAL; CELL LINE; CHEMICAL STRUCTURE; COMPUTER SIMULATION; DOG; GENETICS; LIPOYLATION; METABOLISM; MISSENSE MUTATION; MOUSE; MUTATION; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; XENOPUS LAEVIS;

AMILORIDE; AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE; CELL MEMBRANE; COMPUTER SIMULATION; DOGS; EPITHELIAL SODIUM CHANNEL; ION CHANNEL GATING; LIPOYLATION; MICE; MODELS, MOLECULAR; MUTATION; MUTATION, MISSENSE; OOCYTES; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; SODIUM; SODIUM CHANNEL BLOCKERS; XENOPUS LAEVIS; EPITHELIAL SODIUM CHANNELS;

EID: 77957272702     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.151845     Document Type: Article

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