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AMBRA1 is a tumor suppressor protein that functions as a substrate receptor of the ubiquitin conjugation system with roles in autophagy and the cell cycle regulatory network. The intrinsic disorder of AMBRA1 has thus far precluded its structural determination. To solve this problem, we analyzed the ...
ORGANISM(S): Homo sapiens (Human) 
2023-11-16 | PXD046056 | Pride
Here, using mouse squamous cell carcinoma cells, we report a completely new function for the autophagy protein Ambra1 as the first described ‘spatial rheostat’ controlling the Src/FAK pathway. Ambra1 regulates the targeting of active phospho-Src away from focal adhesions into autophagic structures t...
ORGANISM(S): Mus musculus (Mouse) 
2017-04-04 | PXD006002 | Pride
AMBRA1 interaction mapping in ATRT cellular model to identify potential interaction partners. BT12, BT16, CHLA06 and CHLA266 were used as cellular model. following AP data were analyzed using DIA-NN and interactions were scored against empty FLAG results.
ORGANISM(S): Homo sapiens (Human) 
2023-10-10 | PXD043369 | Pride
T cell receptor (TCR) engagement causes a global cellular response that entrains signaling pathways, cell cycle regulation, and cell death. The molecular regulation of mRNA translation in these processes is poorly understood. During a whole-genome CRISPR screen for regulators of CD95 (Fas/APO-1)-med...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-10-08 | MSV000096042 | MassIVE
Previously, we reported that Ambra1 is a core component of a cytoplasmic trafficking network, acting as a spatial rheostat to control active Src and FAK levels in addition to its critical roles in autophagy during neurogenesis. Here we identify a novel nuclear scaffolding function for Ambra1 that co...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-09 | PXD018745 | Pride
AMBRA1 is a tumour suppressor protein that functions as a substrate receptor in the ubiquitin conjugation system and regulates the stability of D-type cyclins and cell proliferation. Here, we present the cryo-EM structure of cyclin D1 bound AMBRA1-DDB1 complex at 3.55 Å resolution. The structure rev...
ORGANISM(S): Homo sapiens (Human) 
2025-04-17 | PXD062122 | Pride
We sought to identify AMBRA1 interacting proteins and to profile its loss/gain of interactions by mutation using quantitative mass spectrometry.
ORGANISM(S): Homo sapiens (Human) 
2018-07-11 | PXD008005 | Pride
The AMBRA1 E3 ligase adaptor regulates Cyclin D protein stability [U2OS cells]
The AMBRA1 E3 ligase adaptor regulates Cyclin D protein stability [U937 cells]
The AMBRA1 E3 ligase adaptor regulates the stability of cyclin D
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