AMBRA1, a pro-autophagic protein, plays a crucial role in the crosstalk between autophagy and cell proliferation by regulating the stability of c-Myc, a pro-mitotic factor (PMID: 25803737). The structure of the protein is characterized by the presence of WD40-domains in the N-terminal region. The rest of the protein consists of intrinsically disordered regions (IDRs) due to the lack of recognizable protein domains. When autophagy is induced, AMBRA1 is released from the cytoskeletal docking site, initiating autophagosome nucleation by facilitating the ubiquitination of proteins involved in autophagy (PMID:20921139). With the help of TRAF6, AMBRA1 facilitates 'Lys-63'-linked ubiquitination of ULK1, enhancing ULK1 stability and kinase activity (PMID:23524951). Additionally, it serves as a mitophagy activator by interacting with PRKN and LC3 proteins (MAP1LC3A, MAP1LC3B, or MAP1LC3C), potentially aiding in the sequestration of damaged mitochondria into autophagosomes (PMID:21753002, PMID:25215947). AMBRA1 also contains interacting sites for Beclin1 protein (PMID: 23069654, 20921139).
Hetero-Oligomer
Representations
Note*: Right click to select residues and double click to calculate distance distance between the selected residues
