Solution structure of human myeloid-derived growth factor suggests a conserved function in the endoplasmic reticulum

Valeriu Bortnov, Marco Tonelli, Woonghee Lee, Ziqing Lin, Douglas S. Annis, Omar N. Demerdash, Alex Bateman, Julie C. Mitchell, Ying Ge, John L. Markley and Deane F. Mosher ()
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Valeriu Bortnov: University of Wisconsin-Madison
Marco Tonelli: University of Wisconsin-Madison
Woonghee Lee: University of Wisconsin-Madison
Ziqing Lin: University of Wisconsin-Madison
Douglas S. Annis: University of Wisconsin-Madison
Omar N. Demerdash: Biosciences Division, Oak Ridge National Laboratory
Alex Bateman: European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus
Julie C. Mitchell: Biosciences Division, Oak Ridge National Laboratory
Ying Ge: University of Wisconsin-Madison
John L. Markley: University of Wisconsin-Madison
Deane F. Mosher: University of Wisconsin-Madison

Nature Communications, 2019, vol. 10, issue 1, 1-14

Abstract: Abstract Human myeloid-derived growth factor (hMYDGF) is a 142-residue protein with a C-terminal endoplasmic reticulum (ER) retention sequence (ERS). Extracellular MYDGF mediates cardiac repair in mice after anoxic injury. Although homologs of hMYDGF are found in eukaryotes as distant as protozoans, its structure and function are unknown. Here we present the NMR solution structure of hMYDGF, which consists of a short α-helix and ten β-strands distributed in three β-sheets. Conserved residues map to the unstructured ERS, loops on the face opposite the ERS, and the surface of a cavity underneath the conserved loops. The only protein or portion of a protein known to have a similar fold is the base domain of VNN1. We suggest, in analogy to the tethering of the VNN1 nitrilase domain to the plasma membrane via its base domain, that MYDGF complexed to the KDEL receptor binds cargo via its conserved residues for transport to the ER.

Date: 2019
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DOI: 10.1038/s41467-019-13577-5

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