ArticleProtein & cell2012
Crystal structure and functional implication of the RUN domain of human NESCA.
Article in Protein & cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Challenges and progress of neurodrug: bioactivities, production and delivery strategies of nerve growth factor protein.Journal of biological engineering · 2023Review
- Crystal structure of the FYCO1 RUN domain suggests possible interfaces with small GTPases.Acta crystallographica. Section F, Structural biology communications · 2020Article
- The RUFYs, a Family of Effector Proteins Involved in Intracellular Trafficking and Cytoskeleton Dynamics.Frontiers in cell and developmental biology · 2020Review
- Members of the Rusc protein family interact with Sufu and inhibit vertebrate Hedgehog signaling.Development (Cambridge, England) · 2016Article
- PAK1 regulates RUFY3-mediated gastric cancer cell migration and invasion.Cell death & disease · 2015Article
- RUFY, Rab and Rap Family Proteins Involved in a Regulation of Cell Polarity and Membrane Trafficking.International journal of molecular sciences · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NESCA, a newly discovered signaling adapter protein in the NGF-pathway, contains a RUN domain at its N-terminus. Here we report the crystal structure of the NESCA RUN domain determined at 2.0-Å resolution. The overall fold of the NESCA RUN domain comprises nine helices, resembling the RUN domain of RPIPx and the RUN1 domain of Rab6IP1. However, compared to the other RUN domains, the RUN domain of NESCA has significantly different surface electrostatic distributions at the putative GTPase-interacting interface. We demonstrate that the RUN domain of NESCA can bind H-Ras, a downstream signaling molecule of TrkA, with high affinity. Moreover, NESCA RUN can directly interact with TrkA. These results provide new insights into how NESCA participates in the NGF-TrkA signaling pathway.
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Registered trials
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