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Covalent modifier NEDD8 is essential for SCF ubiquitin‐ligase in fission yeast
Author(s) -
Osaka Fumio,
Saeki Mihoro,
Katayama Satoshi,
Aida Noriko,
Tohe Akio,
Kominami Kinichiro,
Toda Takashi,
Suzuki Toshiaki,
Chiba Tomoki,
Tanaka Keiji,
Kato Seishi
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.13.3475
Subject(s) - nedd8 , cullin , biology , ubiquitin ligase , microbiology and biotechnology , schizosaccharomyces pombe , cell division control protein 4 , yeast , schizosaccharomyces , f box protein , ubiquitin , dna ligase , biochemistry , enzyme , saccharomyces cerevisiae , gene
A ubiquitin‐like modifier, NEDD8, is covalently attached to cullin‐family proteins, but its physiological role is poorly understood. Here we report that the NEDD8‐modifying pathway is essential for cell viability and function of Pcu1 (cullin‐1 orthologue) in fission yeast. Pcu1 assembled on SCF ubiquitin‐ligase was completely modified by NEDD8. Pcu1 K713R defective for NEDD8 conjugation lost the ability to complement lethality due to pcu1 deletion. Forced expression of Pcu1 K713R or depletion of NEDD8 in cells resulted in impaired cell proliferation and marked stabilization of the cyclin‐dependent kinase inhibitor Rum1, which is a substrate of the SCF complex. Based on these findings, we propose that covalent modification of cullin‐1 by the NEDD8 system plays an essential role in the function of SCF in fission yeast.