The E3 Ubiquitin Ligase Adaptor Protein Skp1 Is Glycosylated by an Evolutionarily Conserved Pathway That Regulates Protist Growth and Development.

Rahman, Kazi; Zhao, Peng; Mandalasi, Msano; van der Wel, Hanke; Wells, Lance; Blader, Ira J; West, Christopher M

Rahman, Kazi; Zhao, Peng; Mandalasi, Msano; van der Wel, Hanke; Wells, Lance; Blader, Ira J; West, Christopher M.

Afiliação

Rahman K; From the Departments of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, the Department of Microbiology and Immunology, University of O
Zhao P; the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, the Complex Carbohydrate Research Center, Athens, Georgia 30602, and.
Mandalasi M; From the Departments of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
van der Wel H; From the Departments of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
Wells L; the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, the Complex Carbohydrate Research Center, Athens, Georgia 30602, and.
Blader IJ; the Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, the Department of Microbiology and Immunology, University at Buffalo, Buffalo, New York 14214.
West CM; From the Departments of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, the Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, westcm@uga.edu.

J Biol Chem ; 291(9): 4268-80, 2016 Feb 26.

Article em En | MEDLINE | ID: mdl-26719340

Assuntos

Glicosiltransferases/metabolismo; Modelos Moleculares; Processamento de Proteína Pós-Traducional; Proteínas de Protozoários/metabolismo; Proteínas Quinases Associadas a Fase S/metabolismo; Proteínas Ligases SKP Culina F-Box/metabolismo; Toxoplasma/fisiologia; Sequência de Aminoácidos; Células Cultivadas; Sequência Conservada; Evolução Molecular; Deleção de Genes; Glicopeptídeos/química; Glicopeptídeos/metabolismo; Glicosilação; Humanos; Hidroxiprolina/metabolismo; Dados de Sequência Molecular; Oligossacarídeos/química; Oligossacarídeos/metabolismo; Proteínas de Protozoários/química; Proteínas de Protozoários/genética; Proteínas Quinases Associadas a Fase S/química; Proteínas Quinases Associadas a Fase S/genética; Alinhamento de Sequência; Espectrometria de Massas em Tandem; Toxoplasma/enzimologia; Toxoplasma/crescimento & desenvolvimento

Palavras-chave

E3 ubiquitin ligase; SCF-complex; Skp1; Toxoplasma gondii; cytoplasmic glycosylation; glycobiology; glycosyltransferase; parasitology

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Toxoplasma / Modelos Moleculares / Proteínas de Protozoários / Processamento de Proteína Pós-Traducional / Glicosiltransferases / Proteínas Ligases SKP Culina F-Box / Proteínas Quinases Associadas a Fase S Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2016 Tipo de documento: Article

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