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Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase.
Liu, Chang; van Dyk, Dewald; Choe, Vitnary; Yan, Jing; Majumder, Shubhra; Costanzo, Michael; Bao, Xin; Boone, Charles; Huo, Keke; Winey, Mark; Fisk, Harold; Andrews, Brenda; Rao, Hai.
Affiliation
  • Liu C; Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245.
  • van Dyk D; Banting and Best Department of Medical Research, Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
  • Choe V; Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245.
  • Yan J; Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245; State Key Laboratory of Genetic Engineering, Fudan University, Shanghai 200433, China.
  • Majumder S; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210, and.
  • Costanzo M; Banting and Best Department of Medical Research, Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
  • Bao X; Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245.
  • Boone C; Banting and Best Department of Medical Research, Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
  • Huo K; State Key Laboratory of Genetic Engineering, Fudan University, Shanghai 200433, China.
  • Winey M; Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309.
  • Fisk H; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210, and.
  • Andrews B; Banting and Best Department of Medical Research, Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5G 1L6, Canada.
  • Rao H; Institute of Biotechnology, Department of Molecular Medicine, University of Texas Health Science Center, San Antonio, Texas 78245. Electronic address: raoh@uthscsa.edu.
J Biol Chem ; 286(51): 43660-43667, 2011 Dec 23.
Article in En | MEDLINE | ID: mdl-22045814
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein-Tyrosine Kinases / Candida albicans / Gene Expression Regulation, Fungal / Protein Serine-Threonine Kinases / Cell Cycle Proteins / Saccharomyces cerevisiae Proteins / Ubiquitin-Conjugating Enzymes / Ubiquitin-Protein Ligases Limits: Animals / Humans / Male Language: En Journal: J Biol Chem Year: 2011 Type: Article
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein-Tyrosine Kinases / Candida albicans / Gene Expression Regulation, Fungal / Protein Serine-Threonine Kinases / Cell Cycle Proteins / Saccharomyces cerevisiae Proteins / Ubiquitin-Conjugating Enzymes / Ubiquitin-Protein Ligases Limits: Animals / Humans / Male Language: En Journal: J Biol Chem Year: 2011 Type: Article