Skp1-Cullin-F-box-dependent Degradation of Aah1p Requires Its Interaction with the F-box Protein Saf1p

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Glycosylation of Skp1 promotes formation of Skp1-cullin-1-F-box protein complexes in dictyostelium.

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The intracellular levels of many proteins are regulated by ubiquitin-dependent proteolysis. One of the best-characterized enzymes that catalyzes the attachment of ubiquitin to proteins is a ubiquitin ligase complex, Skp1-Cullin-F box complex containing Hrt1 (SCF). We sought to artificially target a protein to the SCF complex for ubiquitination and degradation. To this end, we tested methionine ...

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Glycosylation of Skp1 Affects Its Conformation and Promotes Binding to a Model F-Box Protein

In the social amoeba Dictyostelium, Skp1 is hydroxylated on proline 143 and further modified by three cytosolic glycosyltransferases to yield an O-linked pentasaccharide that contributes to O2 regulation of development. Skp1 is an adapter in the Skp1/cullin1/F-box protein family of E3 ubiquitin ligases that targets specific proteins for polyubiquitination and subsequent proteasomal degradation....

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2007

ISSN: 0021-9258

DOI: 10.1074/jbc.m702425200