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Marte I. Flydal on Muck Rack

Marte I. Flydal

As seen in: Nature
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Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12 - Nature Communications

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By Lorea Velasco-Carneros, Jimena Muntaner, Cesar Santiago, Gloria Gamiz-Arco, Kunwar Jung-KC, David Gil-Cantero, Miguel Marcilla, Juha P. Kallio, José María Valpuesta, Jorge Cuéllar, Lissette Ochoa, Marte I. Flydal, Fernando Moro
| Nature Verified
Abstract Pathogenic variants of the J-domain protein DNAJC12 cause parkinsonism, which is associated with a defective interaction of DNAJC12 with tyrosine hydroxylase (TH), the rate-limiting enzyme in dopamine biosynthesis. In this work, we characterize the formation of the TH:DNAJC12 complex, showing that DNAJC12 binding stabilizes both TH and the variant TH-p.R202H, associated with TH deficiency.
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