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CysMP reveals metal ion-specific metalloproteomes and copper-regulated PGK1 activity in glycolysis

ABSTRACT: Metal ions are crucial in regulating protein functions by coordinating with specific residues, such as cysteine. However, a comprehensive map of metal-specific metalloproteomes in mammals remains elusive, hindering our understanding of their intricate effects. We address this gap by introducing CysMP, a cysteine-centered metalloprotein profiling strategy that uses a cysteine-reactive probe to profile the metalloproteomes of eleven key metal ions. CysMP identified 8895 metal-binding sites across 4150 proteins, enabling quantitative comparisons of cysteine residue interactions with different metals and revealing binding preferences. Notably, zinc and copper ions displayed the broadest protein interaction profiles. Furthermore, CysMP uncovered numerous potential novel metalloproteins. We demonstrate that copper and zinc bind and inhibit 5′-Methylthioadenosine phosphorylase (MTAP), leading to the accumulation of 5’-methylthioadenosine (MTA). Similarly, copper binding inhibits phosphoglycerate kinase 1 (PGK1) activity, downregulating glycolysis. CysMP establishes a rich resource for a dual-specific metalloproteome database, encompassing interactions between metal ions and cysteine residues. Our data not only pave the way for understanding the molecular basis of metalloprotein functions but also hold promise for guiding the development of related therapeutics.

ORGANISM(S): Homo Sapiens

SUBMITTER: Yaoyang Zhang

PROVIDER: PXD055530 | iProX | Wed Sep 04 00:00:00 BST 2024

REPOSITORIES: iProX

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