ArticleThe Journal of biological chemistry2014
Chronophin dimerization is required for proper positioning of its substrate specificity loop.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Article
- Glycolytic flux control by drugging phosphoglycolate phosphatase.Nature communications · 2022Article
- Review
- Sequence specificity between interacting and non-interacting homologs identifies interface residues--a homodimer and monomer use case.BMC bioinformatics · 2015Article
- Chronophin coordinates cell leading edge dynamics by controlling active cofilin levels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Functional Diversity of Haloacid Dehalogenase Superfamily Phosphatases from Saccharomyces cerevisiae: BIOCHEMICAL, STRUCTURAL, AND EVOLUTIONARY INSIGHTS.The Journal of biological chemistry · 2015Article
- Influence of hydrophobic mismatch on the catalytic activity of Escherichia coli GlpG rhomboid protease.Protein science : a publication of the Protein Society · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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Abstract
Mammalian phosphatases of the haloacid dehalogenase (HAD) superfamily have emerged as important regulators of physiology and disease. Many of these enzymes are stable homodimers; however, the role of their dimerization is largely unknown. Here, we explore the function of the obligatory homodimerization of chronophin, a mammalian HAD phosphatase known to dephosphorylate pyridoxal 5'-phosphate (PLP) and serine/threonine-phosphorylated proteins. The exchange of two residues in the murine chronophin homodimerization interface (chronophin(A194K,A195K)) yields a constitutive monomer both in vitro and in cells. The catalytic activity of monomeric chronophin toward PLP is strongly impaired. X-ray crystallographic studies of chronophin(A194K,A195K) revealed that dimer formation is essential for an intermolecular arginine-arginine-tryptophan stacking interaction that positions a critical histidine residue in the substrate specificity loop of chronophin for PLP coordination. Analysis of all available crystal structures of HAD hydrolases that are grouped together with chronophin in the C2a-type structural subfamily uncovered a highly conserved mode of dimerization that results in intermolecular contacts involving the substrate specificity loop. Our results explain how the dimerization of HAD hydrolases contributes to their catalytic efficiency and substrate specificity.
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