Researchers CSIC and University of the Basque Country have discovered a novel mechanism of communication between the proteins that cause ‘ cell suicide ‘or apoptosis: Protein BAX and DRP -1 and lipid cardiolipin acting together to produce a large hole in the outer membrane of mitochondria is lethal for the cell.
The key new study sheds further light on the understanding of ‘ cell suicide ‘ to decipher the new language used by BAX and DRP -1 to communicate and that these two proteins physically interact with each other, as is usual , but do so across the membrane lipids.
These findings have been published in the journal Cell could open new avenues for the rational development of anticancer drugs specifically directed against these components of the cellular apoplectic machinery.
New keys to control cell death protein:
Researchers CSIC have discovered the mechanism by which enzymes called Rsp5 and Ubp2 enable or disable the activity of the proteasome, the multiprotein complex responsible for destroying the protein. Published on the cover of latest issue of the journal Molecular Cell, the research reveals key aspects of the control of cell destruction of proteins that brings more light of how the destruction of defective proteins or those who, after being used, are no longer necessary.
Thus, the finding will better understand how the cell regulates the balance and the genesis of some types of cancer and neurodegenerative diseases like Alzheimer’s, as an abnormal accumulation of proteins that do not degrade may be associated with a decreased activity of proteasomes .
