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

Bortnov, Valeriu; Tonelli, Marco; Lee, Woonghee; Lin, Ziqing; Annis, Douglas S.; Demerdash, Omar N.; Bateman, Alex; Mitchell, Julie C.; Ge, Ying; Markley, John L.; Mosher, Deane F.

doi:10.1038/s41467-019-13577-5

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

Journal Article · 08 December 2019 · Nature Communications

DOI: https://doi.org/10.1038/s41467-019-13577-5 · OSTI ID:1649441

^[1]; Tonelli, Marco ^[1];

^[1];

^[1]; Demerdash, Omar N. ^[2]; Bateman, Alex ^[3];

^[2];

^[1]; Markley, John L. ^[1]; Mosher, Deane F. ^[1]

Univ. of Wisconsin, Madison, WI (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
European Bioinformatics Institute (EMBL-EBI), Hinxton (United Kingdom)

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.

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Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: National Institutes of Health (NIH); National Science Foundation (NSF); USDOE

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1649441

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 10; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Evolutionary Trajectory of the Tet(X) Family: Critical Residue Changes towards High-Level Tigecycline Resistance Cui, Chao-Yue; He, Qian; Jia, Qiu-Lin mSystems, Vol. 6, Issue 3 https://doi.org/10.1128/msystems.00050-21	journal	June 2021
The pH of the Secretory Pathway: Measurement, Determinants, and Regulation Paroutis, Paul; Touret, Nicolas; Grinstein, Sergio Physiology, Vol. 19, Issue 4 https://doi.org/10.1152/physiol.00005.2004	journal	August 2004
An optimized growth medium for increased recombinant protein secretion titer via the type III secretion system Burdette, Lisa Ann; Wong, Han Teng; Tullman-Ercek, Danielle Microbial Cell Factories, Vol. 20, Issue 1 https://doi.org/10.1186/s12934-021-01536-z	journal	February 2021
Vanin 1: Its Physiological Function and Role in Diseases Bartucci, Roberta; Salvati, Anna; Olinga, Peter International Journal of Molecular Sciences, Vol. 20, Issue 16 https://doi.org/10.3390/ijms20163891	journal	August 2019

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