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Protein-metabolite interactomics of carbohydrate metabolism reveal regulation of lactate dehydrogenase. 2023
Kevin G Hicks, and
Ahmad A Cluntun, and
Heidi L Schubert, and
Sean R Hackett, and
Jordan A Berg, and
Paul G Leonard, and
Mariana A Ajalla Aleixo, and
Youjia Zhou, and
Alex J Bott, and
Sonia R Salvatore, and
Fei Chang, and
Aubrie Blevins, and
Paige Barta, and
Samantha Tilley, and
Aaron Leifer, and
Andrea Guzman, and
Ajak Arok, and
Sarah Fogarty, and
Jacob M Winter, and
Hee-Chul Ahn, and
Karen N Allen, and
Samuel Block, and
Iara A Cardoso, and
Jianping Ding, and
Ingrid Dreveny, and
William C Gasper, and
Quinn Ho, and
Atsushi Matsuura, and
Michael J Palladino, and
Sabin Prajapati, and
Pengkai Sun, and
Kai Tittmann, and
Dean R Tolan, and
Judith Unterlass, and
Andrew P VanDemark, and
Matthew G Vander Heiden, and
Bradley A Webb, and
Cai-Hong Yun, and
Pengkai Zhao, and
Bei Wang, and
Francisco J Schopfer, and
Christopher P Hill, and
Maria Cristina Nonato, and
Florian L Muller, and
James E Cox, and
Jared Rutter
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT, USA.
Metabolic networks are interconnected and influence diverse cellular processes. The protein-metabolite interactions that mediate these networks are frequently low affinity and challenging to systematically discover. We developed mass spectrometry integrated with equilibrium dialysis for the discovery of allostery systematically (MIDAS) to identify such interactions. Analysis of 33 enzymes from human carbohydrate metabolism identified 830 protein-metabolite interactions, including known regulators, substrates, and products as well as previously unreported interactions. We functionally validated a subset of interactions, including the isoform-specific inhibition of lactate dehydrogenase by long-chain acyl-coenzyme A. Cell treatment with fatty acids caused a loss of pyruvate-lactate interconversion dependent on lactate dehydrogenase isoform expression. These protein-metabolite interactions may contribute to the dynamic, tissue-specific metabolic flexibility that enables growth and survival in an ever-changing nutrient environment.
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