Related Experiment Video

Updated: Jan 2, 2026

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
16:43

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

13.5K

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

Valeriu Bortnov1, Marco Tonelli2,3, Woonghee Lee2,3

  • 1Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.

Nature Communications
|December 11, 2019
PubMed

Insights

Human myeloid-derived growth factor (hMYDGF) has an unknown structure and function. This study reveals its NMR solution structure, suggesting a role in ER-bound cargo transport.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Human myeloid-derived growth factor (hMYDGF) is a protein involved in cardiac repair.
  • Its structure and function remain largely unknown despite homologous proteins existing across eukaryotes.
  • hMYDGF possesses a C-terminal endoplasmic reticulum (ER) retention sequence (ERS).

Purpose of the Study:

  • To determine the solution structure of human myeloid-derived growth factor (hMYDGF).
  • To elucidate the potential function of hMYDGF based on its structural features and conserved residues.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the solution structure of hMYDGF.
  • Structural analysis involved identifying secondary structural elements and mapping conserved residues.

Main Results:

  • The NMR solution structure of hMYDGF was determined, revealing a fold comprising a short alpha-helix and ten beta-strands arranged in three beta-sheets.
  • Conserved residues were identified in the ERS, loops opposite the ERS, and a cavity surface.
  • The determined fold is similar to the base domain of VNN1.

Conclusions:

  • The structure of hMYDGF suggests a potential role in binding cargo via conserved residues.
  • It is hypothesized that hMYDGF, when complexed with the KDEL receptor, facilitates cargo transport to the ER.
  • This finding provides insights into the molecular mechanisms of ER-bound protein transport and cellular repair.

More Related Videos

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

9.3K
Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum07:49

Spontaneous Formation and Rearrangement of Artificial Lipid Nanotube Networks as a Bottom-Up Model for Endoplasmic Reticulum

Published on: January 22, 2019

8.2K

Related Concept Videos

Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.7K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
16.5K
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
20.8K
Endoplasmic Reticulum01:39

Endoplasmic Reticulum

The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
105.4K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
4.9K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.5K