Ubiquitin Structure & Function: Difference between revisions
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This conjugate formation is the most important process in protein degradation as it officially targets the protein for degradation. Polyubiquitinylation refers to the addition of several ubiquitin molecules to a single lysine residue on a protein. Isopeptide bonds are formed between the carboxyl-terminus of one ubiquitin and a lysine residue on an adjacent ubiquitin. | This conjugate formation is the most important process in protein degradation as it officially targets the protein for degradation. Polyubiquitinylation refers to the addition of several ubiquitin molecules to a single lysine residue on a protein. Isopeptide bonds are formed between the carboxyl-terminus of one ubiquitin and a lysine residue on an adjacent ubiquitin. | ||
=Diseases= | =Diseases= | ||
There are numerous diseases that may develop as a result of ubiquitin abnormalities. | There are numerous diseases that may develop as a result of ubiquitin abnormalities. There are two disease categories possible in non-lethal states. One being the result of function loss and the other being function gain. Loss of function may occur due to a target substrate mutation or a mutation in a ubiquitin enzyme causing protein stabilization and a decrease in protein degradation. Function gain, on the other hand, results in an increase in protein degradation. | ||
Cancer may result from either cases. Oncoproteins may become stabilized while tumor suppressor genes may become destabilized. Liddle's Syndrome is a type of early-onset hypertension<ref name="liddles">PMID: 8521520</ref>. Sodium ions and water are excessively reabsorbed caused by E3 ligase non-recognition. | |||
=References= | =References= | ||
<references/> | <references/> | ||
