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Activity of a ubiquitin ligase adaptor is regulated by disordered insertions in its arrestin domain.
Baile, Matthew G; Guiney, Evan L; Sanford, Ethan J; MacGurn, Jason A; Smolka, Marcus B; Emr, Scott D.
Affiliation
  • Baile MG; Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
  • Guiney EL; Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
  • Sanford EJ; Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
  • MacGurn JA; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37212.
  • Smolka MB; Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
  • Emr SD; Weill Institute for Cell and Molecular Biology and Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Mol Biol Cell ; 30(25): 3057-3072, 2019 12 01.
Article in En | MEDLINE | ID: mdl-31618110
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Transcription Factors / Protein Transport / Saccharomyces cerevisiae Proteins / DNA-Binding Proteins / Endocytosis Type of study: Prognostic_studies Language: En Journal: Mol Biol Cell Journal subject: BIOLOGIA MOLECULAR Year: 2019 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Transcription Factors / Protein Transport / Saccharomyces cerevisiae Proteins / DNA-Binding Proteins / Endocytosis Type of study: Prognostic_studies Language: En Journal: Mol Biol Cell Journal subject: BIOLOGIA MOLECULAR Year: 2019 Document type: Article