N-glycosylation determines the abundance of the transient receptor potential channel TRPP2

Journal of Biological Chemistry

Volumn 289, Issue 21, 2014, Pages 14854-14867

  Hofherr, Alexis ^a,b   Wagner, Claudius ^a   Fedeles, Sorin ^c   Somlo, Stefan ^c   Köttgen, Michael ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b UNIVERSITY OF FREIBURG   (Germany)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; BIOSYNTHESIS; ESTERIFICATION; MASS SPECTROMETRY; POLYSACCHARIDES; PROTEINS; TRIMMING;

EXTRACELLULAR LOOPS; GENETIC INTERACTION; LYSOSOMAL DEGRADATION; N-LINKED GLYCOSYLATION; NON-SELECTIVE CATION CHANNELS; POLYCYSTIC KIDNEY DISEASE; PROTEIN EXPRESSIONS; TRANSIENT RECEPTOR POTENTIAL CHANNELS;

GLYCOSYLATION;

ASPARAGINE; GLUCOSIDASE; GLUCOSIDASE IIBETA; TRANSIENT RECEPTOR POTENTIAL CHANNEL 2; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; AUTOSOMAL DOMINANT POLYCYSTIC LIVER DISEASE; BIOGENESIS; CONTROLLED STUDY; GENE; GENE INTERACTION; GENE MUTATION; GENETIC CODE; GLYCOSYLATION; HUMAN; HUMAN CELL; LIVER POLYCYSTIC DISEASE; LYSOSOME; MASS SPECTROMETRY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PRKCSH GENE; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN STABILITY; TRPP2 GENE;

GENETIC DISEASES; GLYCOSYLATION; KIDNEY; LYSOSOMES; TRP CHANNELS;

ANIMALS; ASPARAGINE; BINDING SITES; BLOTTING, WESTERN; CELL LINE; CELLS, CULTURED; GLUCOSIDASES; GLYCOSYLATION; HEK293 CELLS; HELA CELLS; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LYSOSOMES; MASS SPECTROMETRY; MICE; MICE, KNOCKOUT; MICROSCOPY, FLUORESCENCE; MUTATION; POLYCYSTIC KIDNEY, AUTOSOMAL DOMINANT; PROTEIN-SERINE-THREONINE KINASES; PROTEOLYSIS;

EID: 84901411100     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.562264     Document Type: Article

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