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- W4243478421 abstract "(Molecular Cell 35, 841–855; September 24, 2009) In the above article, the affiliations were originally listed incorrectly. The authors and affiliations list should have appeared as it does in this Erratum. We regret any inconvenience this may have caused. Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell MovementChen et al.Molecular CellSeptember 24, 2009In BriefCul3, a Cullin family scaffold protein, is thought to mediate the assembly of a large number of SCF (Skp1-Cullin1-F-box protein)-like ubiquitin ligase complexes through BTB domain substrate-recruiting adaptors. Cul3 controls early embryonic development in several genetic models through mechanisms not understood. Very few functional substrate/adaptor pairs for Cul3 ubiquitin ligases have been identified. Here, we show that Cul3 knockdown in human cells results in abnormal actin stress fibers and distorted cell morphology, owing to impaired ubiquitination and degradation of small GTPase RhoA. Full-Text PDF Open Archive" @default.
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- W4243478421 date "2011-12-01" @default.
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- W4243478421 title "Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell Movement" @default.
- W4243478421 doi "https://doi.org/10.1016/j.molcel.2011.12.001" @default.
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