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Affinity purification coupled to mass spectrometry is often used as a complementary technique to BioID experiments, and the data presented here complements another project. To infer processes involving Ku70, we used AP-MS to identify candidate proteins that may interact with Ku70 and compared these ...
ORGANISM(S): Homo sapiens (Human) 
2019-01-03 | PXD010930 | Pride
We conducted proximity-dependent biotin identification (BioID) using wild-type Ku70 in HEK293 cells. Ku70 is part of a protein complex known as Ku, which is involved in a variety of functions throughout the cell. By identifying candidate protein interactors, we can infer new cellular processes that ...
ORGANISM(S): Homo sapiens (Human) 
2019-01-03 | PXD010931 | Pride
To determine if the proximity-dependent biotin identification (BioID2) technique could identify and map domain and region specific protein interactors, we conducted BioID2 with various segments of the Ku70 protein in the HEK293 cell line and compared the different datasets. To our knowledge, this is...
ORGANISM(S): Homo sapiens (Human) 
2021-04-22 | PXD020165 | Pride
Introduction: Ubiquitination is a major regulatory process that is often dysregulated in carcinogenesis. The C-terminal to LisH (CTLH) complex is a multi-subunit E3 ubiquitin ligase that has been shown to exert tumor-promoting and tumor-suppressing functions. Its core scaffolding subunit, RanBP9, h...
ORGANISM(S): Mus musculus (Mouse) 
2026-09-21 | PXD081521 | Pride
To identify Ku70 phosphoS155-specific proximal protein interactors, we used the proximity-dependent biotin identification (BioID2) technique with wild-type Ku70, Ku70 S155A, and Ku70 S155D in the doxycycline-inducible T-REx 293 cell line and compared the different datasets.
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD025581 | Pride
The human CTLH complex is a newly discovered multi-subunit E3 ligase. At present, only a few of its ubiquitination targets are known. Here, we use proteomic techniques in RanBPM-depleted HeLa cells to identify ubiquitination substrates of the CTLH complex. First, global proteomics determined protein...
ORGANISM(S): Homo sapiens (Human) 
2021-08-13 | PXD024872 | Pride
The Pro/N-degron recognizing C-terminal to LisH (CTLH) complex is an E3 ligase of emerging interest in the developmental field and for targeted protein degradation (TPD) modalities. The human CTLH complex forms distinct supramolecular ring-shaped structures dependent on the multimerization of WDR26 ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-03-14 | MSV000094320 | MassIVE
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