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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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...
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors are of three kinds RI, RII, and RIII. The RI...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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 affinity and are together...
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...
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
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Inactive and highly active, proteolytically processed transglutaminase-5 in epithelial cells.

Valentina Pietroni1, Sabrina Di Giorgi, Andrea Paradisi

  • 1Biochemistry Laboratory, Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, Rome, Italy.

The Journal of Investigative Dermatology
|May 30, 2008
PubMed
Summary

Transglutaminases (TGs) are enzymes crucial for biological processes. This study reveals that TG5 requires proteolytic processing to achieve high enzymatic activity, unlike its full-length form.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Transglutaminases (TGs) are calcium-dependent enzymes catalyzing transamidation reactions.
  • TGs play roles in coagulation, wound healing, cell death, and keratinocyte differentiation.
  • Transglutaminase 5 (TG5) is a recently identified member with limited functional characterization.

Purpose of the Study:

  • To investigate the functional characterization of Transglutaminase 5 (TG5).
  • To determine the enzymatic activity of TG5 in different forms.

Main Methods:

  • Expression of TG5 in baculovirus and mammalian epithelial cell systems.
  • Analysis of TG5 proteolytic processing.
  • Assay of enzymatic activity for full-length and processed TG5.

Main Results:

  • TG5 undergoes proteolytic processing in both baculovirus and mammalian cell expression systems.
  • The full-length TG5 enzyme exhibits low enzymatic activity.
  • A 53-kDa proteolytically processed form of TG5 demonstrates significantly high enzymatic activity.

Conclusions:

  • Proteolytic processing is essential for the activation of Transglutaminase 5 (TG5).
  • The activated 53-kDa form of TG5 is a highly active enzyme.
  • This finding clarifies the functional mechanism of TG5 within the transglutaminase family.