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

Author

Listed:
  • Valeriu Bortnov

    (University of Wisconsin-Madison)

  • Marco Tonelli

    (University of Wisconsin-Madison
    National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison)

  • Woonghee Lee

    (University of Wisconsin-Madison
    National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison)

  • Ziqing Lin

    (University of Wisconsin-Madison
    Human Proteomics Program, 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
    Human Proteomics Program, University of Wisconsin-Madison)

  • John L. Markley

    (University of Wisconsin-Madison
    National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison)

  • Deane F. Mosher

    (University of Wisconsin-Madison
    University of Wisconsin-Madison)

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.

Suggested Citation

  • Valeriu Bortnov & Marco Tonelli & Woonghee Lee & Ziqing Lin & Douglas S. Annis & Omar N. Demerdash & Alex Bateman & Julie C. Mitchell & Ying Ge & John L. Markley & Deane F. Mosher, 2019. "Solution structure of human myeloid-derived growth factor suggests a conserved function in the endoplasmic reticulum," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13577-5
    DOI: 10.1038/s41467-019-13577-5
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    Cited by:

    1. Linda Große-Segerath & Paula Follert & Kristina Behnke & Julia Ettich & Tobias Buschmann & Philip Kirschner & Sonja Hartwig & Stefan Lehr & Mortimer Korf-Klingebiel & Daniel Eberhard & Nadja Lehwald-T, 2024. "Identification of myeloid-derived growth factor as a mechanically-induced, growth-promoting angiocrine signal for human hepatocytes," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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