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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
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Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
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G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
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Gasdermins: pore-forming activities and beyond.

Zengzhang Zheng1,2,3, Wanyan Deng1,2,3, Xiwen Lou3

  • 1The Joint Center for Infection and Immunity between Guangzhou Institute of Pediatrics, Guangzhou Women and Children's Medical Center, Guangzhou, 510623, China.

Acta Biochimica Et Biophysica Sinica
|April 16, 2020
PubMed
Summary

Gasdermins (GSDMs) are a protein family crucial for inflammatory cell death. Mutations in GSDM genes are linked to autoimmune diseases and cancers, highlighting their disease relevance.

Keywords:
deafnessgasderminpore-forming proteinpyroptosistumorigenesis

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Area of Science:

  • Molecular Biology
  • Immunology
  • Genetics

Background:

  • Gasdermins (GSDMs) are a vertebrate-specific protein superfamily.
  • Most GSDMs share a conserved two-domain structure and autoinhibitory mechanism.
  • DFNB59 (Pejvakin) is an exception within the human GSDM family.

Purpose of the Study:

  • To review current knowledge on Gasdermin (GSDM) expression and regulation.
  • To elucidate the roles of GSDMs in inflammatory cell death, tumorigenesis, and related diseases.

Main Methods:

  • Literature review of GSDM research.
  • Analysis of GSDM structure and function.
  • Examination of GSDM involvement in disease pathology.

Main Results:

  • Released N-terminal domains of GSDMs exhibit pore-forming activity, inducing inflammatory cell death.
  • GSDM mutations are associated with autoimmune disorders and cancers.
  • GSDMs play significant roles in inflammation and disease development.

Conclusions:

  • GSDMs are key regulators of inflammatory cell death.
  • Dysregulation of GSDMs contributes to autoimmune diseases and cancer.
  • Further research into GSDMs is vital for understanding and treating related diseases.