F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex

Article Abstract:

Experiment was conducted to explore the role of Skp1 and F-box proteins in ubiquitination through in vitro reconstruction of the Sic1 ubiquitination pathway. Skp1 functions to recruit Cdc-4 into a Cdc53/Cdc-34 complex and enhances recognition of Sic1 by Cdc4, the latter interaction requiring Sic1 phosphorylation. In comparison, Grr1 does not interact with Sic1 but recruits phosphorylated Cln1 and Cln2 into Skp1/Cdc53 complexes. Results suggest that F-box proteins function as receptors that recruit substrates into a Skp1/Cdc53/Cdc34 complex for ubiquitination.

Saccharomyces, Protein kinases, Cell receptors, Recombinant proteins, Ubiquitin

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How the cyclin became a cyclin: regulated proteolysis in the cell cycle

Article Abstract:

Previous studies have found that cyclins and cyclin-dependent kinases (Cdks) perform a vital role in regulating cell cycle transitions. It was also observed that cyclins and Cdks collaborate with ubiquitin-mediated proteolysis to create a logical framework for cell cycle regulation. Furthermore, researches have found that two E3 complexes are responsible for regulating proteolysis. These include the cyclosome/anaphase=promoting complex and the SCF complex.

Analysis, Physiological aspects, Cell research, Cytological research

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SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box

Article Abstract:

A yeast gene called SKP1 has been identified as a component of the G1/S and G2/M proteolysis pathways. In addition, the gene is known to be involved in the proteolysis of the Sic1p protein through its interactions with Cdc4p and associates with cyclins A and F and with kinetochores in yeast. These indicate a connection between regulation of proteolysis in different stages of the cell cycle.

Genetic aspects, Carrier proteins, Transport proteins, Yeast, Yeast (Food product)

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