Proteomics

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CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation

ABSTRACT: HEK293T cells were co-transfected with StrepII-FLAG-tagged DCAF12 and HA-tagged CUL4A, grown for 48 h, harvested, and lysed as described above. In the first step, Strep-TactinXT Superflow resin (IBA Lifesciences, Gottingen, Germany) was used to purify proteins associated with StrepII-FLAG-tagged subsrtrate receptors. In the second step, eluates from the previous step were used for immunoprecipitation of HA-CUL1/4A-associated proteins. Eluates from both steps were analyzed by LC-MS/MS at the Proteomics facility of Biotechnology and Biomedicine Center of the Academy of Sciences and Charles University (BIOCEV) in Vestec, Czech Republic. Further details are provided in Supplementary methods.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Lukas Cermak  

PROVIDER: MSV000097470 | MassIVE | Tue Apr 01 06:09:00 BST 2025

SECONDARY ACCESSION(S): PXD067954

REPOSITORIES: MassIVE

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CRL4-DCAF12 Ubiquitin Ligase Controls MOV10 RNA Helicase during Spermatogenesis and T Cell Activation.

Lidak Tomas T   Baloghova Nikol N   Korinek Vladimir V   Sedlacek Radislav R   Balounova Jana J   Kasparek Petr P   Cermak Lukas L  

International journal of molecular sciences 20210520 10

Multisubunit cullin-RING ubiquitin ligase 4 (CRL4)-DCAF12 recognizes the C-terminal degron containing acidic amino acid residues. However, its physiological roles and substrates are largely unknown. Purification of CRL4-DCAF12 complexes revealed a wide range of potential substrates, including MOV10, an "ancient" RNA-induced silencing complex (RISC) complex RNA helicase. We show that DCAF12 controls the MOV10 protein level via its C-terminal motif in a proteasome- and CRL-dependent manner. Next,  ...[more]

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