Positive Samples: U-87MG, HeLa, Jurkat, MCF7; Cellular Location: Cytoplasmic vesicle, autophagosome
Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. Beclin-1, a principal regulator of autophagosome formation, is in turn regulated by Ambra1. Ambra1 associates with Beclin-1 through a region near its center as determined by yeast two-hybrid assay. Null mutations in this gene in mice resulted in embryonic lethality with severe neural tube defects associated with autophagy impairment, accumulation of ubiquitinated proteins, unbalanced cell proliferation and excessive apoptotic death. Furthermore, down-regulation of Ambra1 in cultured cells though RNA interference decreased the level of rapamycin- and nutrient starvation-induced autophagy. Multiple isoforms of Ambra1 are known to exist.
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Protein Aliases: activating molecule in beclin-1-regulated autophagy; activating molecule in Beclin1-regulated autophagy; Activating molecule in BECN1-regulated autophagy protein 1; autophagy/beclin-1 regulator 1; DDB1 and CUL4 associated factor 3; ischemia related factor NYW-1; WD repeat domain 94
Gene Aliases: 2310079H06Rik; A130023A14; AA474864; AMBRA1; AV021921; D030051N19Rik; DCAF3; KIAA1736; mKIAA1736; Nyw1; WDR94