The yeast Npi1/Rsp5 ubiquitin ligase lacking its N-terminal C2 domain is competent for ubiquitination but not for subsequent endocytosis of the gap1 permease.

Springael, J Y; De Craene, J O; André, B

Springael, J Y; De Craene, J O; André, B.

Affiliation

Springael JY; Laboratoire de Physiologie Cellulaire et de Génétique des Levures, Université Libre de Bruxelles-Campus Plaine CP244, Bd du triomphe, Bruxelles, B-1050, Belgium.

Biochem Biophys Res Commun ; 257(2): 561-6, 1999 Apr 13.

Article in En | MEDLINE | ID: mdl-10198251

Subject(s)

Endocytosis; Ligases/metabolism; Membrane Transport Proteins/metabolism; Saccharomyces cerevisiae Proteins; Saccharomyces cerevisiae/enzymology; Sequence Deletion/genetics; Ubiquitin-Protein Ligase Complexes; Amino Acid Substitution; Amino Acid Transport Systems; Animals; Blotting, Western; Conserved Sequence/genetics; Cysteine/genetics; Cysteine/metabolism; Down-Regulation/drug effects; Endocytosis/drug effects; Endosomal Sorting Complexes Required for Transport; Enzyme Stability; Humans; Ligases/chemistry; Ligases/genetics; Molecular Weight; Quaternary Ammonium Compounds/pharmacology; Saccharomyces cerevisiae/cytology; Saccharomyces cerevisiae/growth & development; Saccharomyces cerevisiae/metabolism; Ubiquitin-Protein Ligases

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Collection: 01-internacional Database: MEDLINE Main subject: Membrane Transport Proteins / Saccharomyces cerevisiae / Sequence Deletion / Saccharomyces cerevisiae Proteins / Ubiquitin-Protein Ligase Complexes / Endocytosis / Ligases Limits: Animals / Humans Language: En Journal: Biochem Biophys Res Commun Year: 1999 Document type: Article Affiliation country: Belgium

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