Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation
Suparno Nandi, Mortezaali Razzaghi, Dhiraj Srivastava, Mishtu Dey
Abstract
7.5. However, the PTM mimetics exist as a mixture of tetramer and dimer, indicating that physiologically dimeric fraction is important and might be necessary for the modified PKM2 to translocate into the nucleus. Thus, our findings provide insight into how PTMs and pH regulate PKM2 and offer a broader understanding of its intricate allosteric regulation mechanism by phosphorylation or acetylation.
Topics & Concepts
Allosteric regulationPKM2AcetylationPhosphorylationBiochemistryPyruvate kinaseChemistryTetramerGlycolysisKinaseCell biologyBiologyEnzymeGeneCancer, Hypoxia, and MetabolismMetabolism, Diabetes, and CancerMitochondrial Function and Pathology