A vacuolar carboxypeptidase mutant of Arabidopsis thaliana is degraded by the ERAD pathway independently of its N-glycan

Biochemical and Biophysical Research Communications

Volumn 393, Issue 3, 2010, Pages 384-389

  Yamamoto, Masaya ^a   Kawanabe, Mitsuyoshi ^a   Hayashi, Yoko ^a   Endo, Toshiya ^a   Nishikawa, Shuh ichi ^a  

^a NAGOYA UNIVERSITY   (Japan)

Author keywords

Arabidopsis thaliana; Endoplasmic reticulum (ER); ER associated degradation (ERAD); Serine carboxypeptidase

Indexed keywords

CARBOXYPEPTIDASE C; CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 48; GLYCAN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MUTANT PROTEIN; PROTEASOME; UNCLASSIFIED DRUG;

ARABIDOPSIS; ARTICLE; CELL VACUOLE; CONTROLLED STUDY; DEGRADATION KINETICS; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENZYME DEGRADATION; NONHUMAN; NUCLEOTIDE SEQUENCE; ORTHOLOGY; PLANT CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; WILD TYPE; YEAST CELL;

AMINO ACID SEQUENCE; ARABIDOPSIS; CATHEPSIN A; ENDOPLASMIC RETICULUM; GREEN FLUORESCENT PROTEINS; MOLECULAR SEQUENCE DATA; POLYSACCHARIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; VACUOLES;

ARABIDOPSIS THALIANA;

EID: 77949272203     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.02.001     Document Type: Article

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