In stressful situations, CHIP often appears as a so-called homodimer, that is, a mixture of two identical proteins, the task of which is to destroy unfolded proteins. It is the natural cell cleansing process. CHIP frequently interacts with other helper proteins and also controls insulin receptor signal transduction. CHIP can bind to and destroy it, thus preventing activation of life-prolonging gene products. Therefore, we cannot live forever.
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CHIP plays very important roles in our bodies, but it turns out that it works better when performed alone rather than in pairs. Show it Scientists from the University of CologneWho described the search results in molecular cell.
Chip shape is important
Experiments with nematodes Certain types are elegant Human cells showed that CHIP could be tagged with ubiquitin, preventing its dimer formation. In this form, the monomer is more efficient in regulating insulin signaling.
Whether CHIP functions alone or as a pair depends on the state of the cell. There are a lot of denatured proteins under stress in addition to the helper proteins that bind to CHIP and prevent ubiquitin from self-labelling. After CHIP is effective in purging damaged proteins, it can also mark degradation co-proteins. For the body to function efficiently, there must be a balance between the monochromatic and dim forms of the slide.
a. Thorsten Hoppe from the University of Cologne says:
Interestingly, the monomer-dimer balance of CHIP appears to be perturbed in neurodegenerative diseases.
This is the case in myeloid ataxia, in which different sites of CHIP are mutated and the protein acts primarily as dimers. If the body’s balance could be shifted toward monomers, it would be possible to cure the disease—at least in theory.
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The scientists now want to search for proteins, or receptors, to which the CHIP monomer binds and thus regulates its function. It is also important to identify the tissues and organs in which CHIP monomers or dimers are most abundant. This knowledge can be of great therapeutic importance.
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