Rapid degradation of the G1 cyclin Cln2 induced by CDK-Dependent phosphorylation

Science

Volumn 271, Issue 5255, 1996, Pages 1597-1601

  Lanker, Stefan ^a   Valdivieso, M Henar ^b   Wittenberg, Curt ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF SALAMANCA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLINE; PROTEIN KINASE; CLN2 PROTEIN, YEAST; CYCLIN DEPENDENT KINASE 1; FUNGAL PROTEIN;

ARTICLE; CELL CYCLE G1 PHASE; CONTROLLED STUDY; ENZYME SUBUNIT; EUKARYOTE; NONHUMAN; PRIORITY JOURNAL; PROTEIN METABOLISM; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; YEAST; AMINO ACID SEQUENCE; CYTOLOGY; ENZYME ACTIVATION; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; PHENOTYPE; PHOSPHORYLATION; SACCHAROMYCES CEREVISIAE;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; CDC28 PROTEIN KINASE, S CEREVISIAE; CYCLINS; ENZYME ACTIVATION; FUNGAL PROTEINS; G1 PHASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENOTYPE; PHOSPHORYLATION; SACCHAROMYCES CEREVISIAE;

EID: 0029670193     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.271.5255.1597     Document Type: Article

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39. 4T3S, thus creating the same deletion within the cyclin box as in Cln2Δxs (9).
40. 3 construct, M Guaderrama for expert technical assistance, L. Hengst, C. McGowan, P. Russell, and D. Stuart for helpful discussions and critical reading of the manuscript, and S Reed for his encouragement at a critical juncture. Supported by U.S. Public Health Services grant GM43487 to C W. S.L acknowledges Swiss National Science Foundation and Human Frontier Science Program fellowships. M.H.V. was supported by the Fundación Ramón Areces, Madrid, Spain