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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Cell death is an essential process where the body gets rid of old or damaged cells. Cell proliferation and death need to be balanced, as an imbalance between the two may lead to cancer or autoimmune diseases.
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Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Related Experiment Video

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A β-glucuronidase GUS Based Cell Death Assay
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Keeping the Death Protein in Check.

Longfei Wang1, Hao Wu1

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA; Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.

Immunity
|July 18, 2019
PubMed
Summary

Researchers reveal the crystal structures of human and mouse Gasdermin D, an inflammatory cell death executor. These findings clarify Gasdermin D

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Gasdermin D (GSDMD) is a key protein mediating programmed inflammatory cell death, a critical process in immunity and disease.
  • Understanding the structural basis of GSDMD regulation is essential for developing targeted therapies.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying Gasdermin D autoinhibition and activation.
  • To provide atomic-level insights into the full-length human and mouse Gasdermin D structures.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structures of full-length human and mouse Gasdermin D.

Main Results:

  • The crystal structures reveal the molecular details of Gasdermin D in its auto-inhibited conformation.

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  • These structures provide a framework for understanding how Gasdermin D is activated to permeabilize membranes.

    • Conclusions:

    • The reported structures offer unprecedented insights into Gasdermin D's regulatory mechanisms.
    • This structural information will be invaluable for the rational design of novel therapeutics targeting Gasdermin D in inflammatory diseases.