The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families

Article Abstract:

Recent research has shown that Elongin BC complex binds to a functional BC box present in the SOCS box. It appears that the Elongin BC complex is a part of a multiprotein SOCS-1 complex that attenuates Jak/STAT signaling by binding to Jak2 and inhibiting Jak2 kinase. It seems to interact with the SOCS box, the so that it can increase expression of the SOCS-1 protein by inhibiting degradation of the protein. Elongin BC appears to be a multifunctional regulatory complex that can control a number of pathways in a cell by interacting with a short degenerate sequence motif that is in many proteins. The Elongin BC complex was identified first as a positive regulator of RNA polymerase II (Pol II ) elongation factor Elongin A and later as a part of the multiprotein von Hippel-Lindau (VHL) tumor suppressor complex. The SOCS-box pattern can be seen in the suppressor of cytokine signaling-1 protein and in an assortment of other proteins of the repeat families of ras, SOCS, SPRY domain, ankyrin and WD-40 repeat.

Observations, Proteins, Cellular signal transduction, Tumor suppressor genes, Protein separation

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The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2

Article Abstract:

The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase has been found to activate Rub1 modification of cullins Cdc53 and Cul2. The mechanism involves the dedicated E2Rub1 conjugating enzyme Ubc12. Findings show Rbx1 to be a common component of enzyme systems responsible for ubiquitin and Rub1 modification of target proteins. An in vitro Rub1 modification system of purified recombinant S. cerevisiae Rub1-activating enzyme Uba3/Ula1 and S. cerevisae Rub1-conjugating enzyme Ubc12 was put together.

Statistical Data Included, Research, Physiological aspects, Genetic aspects, Enzymes, Cytochemistry, Saccharomyces, Binding sites (Biochemistry), Active sites (Biochemistry), Ligases, Conjugation (Biology), Conjugation (Reproduction)

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