Abstract
Phafin2 is a peripheral protein that triggers cellular signaling from endosomal and lysosomal compartments. The specific subcellular localization of Phafin2 is mediated by the presence of a tandem of phosphatidylinositol 3-phosphate (PtdIns3P)-binding domains, the pleckstrin homology (PH) and the Fab-1, YOTB, Vac1, and EEA1 (FYVE) domains. The requirement for both domains for binding to PtdIns3P still remains unclear. To understand the molecular interactions of the Phafin2 PH domain in detail, we report its nearly complete 1H, 15N, and 13C backbone resonance assignments.
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Data availability
The assignments of resonances of the Phafin2 PH domain were deposited in the Biological Magnetic Resonance Bank database under accession number 26309.
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Acknowledgements
We thank Dr. Janet Webster for assistance during preparation of the manuscript. This work was funded by the 4-VA Collaborative Research Program and by the Virginia Academy of Science Mary Louis Andrews for Cancer Research (to D.G.S.C.). T.T. was supported by the Joseph Frank Hunkler Memorial Fellowship. Some of the NMR data presented in this work was collected using an NMR instrument purchased with an NIH High End Instrumentation grant (S10 RR023035), which is housed in the Biomolecular Magnetic Resonance Facility at the University of Virginia.
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JFE and DGSC, research design; TT, purified recombinant protein; JFE, TT, and NS, performed and analyzed two-dimensional NMR experiments; JFE, performed and analyzed three-dimensional NMR experiments; DGSC, wrote the manuscript with contributions from all authors.
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Ellena, J.F., Tang, TX., Shanaiah, N. et al. Backbone 1H, 15N, and 13C resonance assignments of the Phafin2 pleckstrin homology domain. Biomol NMR Assign 16, 27–30 (2022). https://doi.org/10.1007/s12104-021-10054-3
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DOI: https://doi.org/10.1007/s12104-021-10054-3