Apoptosis regulator BAX, otherwise called BCL-2-like protein 4, is a protein that’s encoded by the BAX DNA when present in humans. BAX is part of the Bcl2-associated X protein family and has its BH3 domain on the contradictory side to the section and asymmetric structures. Members of the bcl2 family form hetero or homodimers and behave like pro or anti-apoptotic regulators associated with a wide range of cellular processes.
Most of BAX is found in the cytosol in vital mammalian cells, yet after signalling apoptotic initiation, BAX goes through a conformational move. After apoptotic induction, BAX becomes organelle membrane related, and specifically, mitochondrial tissue related.
Different abiotic elements stimulate BAX activation, such as: Heat, High or low pH, Hydrogen peroxide, Mitochondrial membrane redesigning.
Additionally, it can also be initiated by binding BCL-2 just as other non-BCL-2 proteins, for instance, Bif-1 and p53.
Bcl-2-related X protein appeared to act together with other human protein genes, including: Bcl-2, BCL2L1, BCL2A1, SH3GLB1, SLC25A4, VDAC1, TCTP, YWHAQ. Bid, Bim, Puma, Noxa, Mfn2, Cholesterol, Cardiolipin.
The BAX gene was the first recognized favorable apoptotic member from the Bcl-2 protein family. Members of the Bcl-2 family share at least one of the four distinct homology areas entitled the Bcl-2 homology (BH) areas (BH1, BH2, BH3, and BH4) can frame hetero or homodimers.
BAX Clinical significance
Tumor suppressor protein p53 upregulates BAX expression, and the BAX has been demonstrated to be engaged with p53-mediated apoptosis. The p35 protein is a transcription element, when initiated as a component of the cell’s reaction to stress, manages numerous target genes, including BAX.