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Related Concept Videos

Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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The Unfolded Protein Response01:37

The Unfolded Protein Response

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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...
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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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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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ERp57/PDIA3: new insight.

Silvia Chichiarelli1, Fabio Altieri2, Giuliano Paglia2

  • 1Department of Biochemical Sciences "A.Rossi-Fanelli", Sapienza University of Rome, P.le A.Moro 5, 00185, Rome, Italy. silvia.chichiarelli@uniroma1.it.

Cellular & Molecular Biology Letters
|February 3, 2022
PubMed
Summary

The ERp57/PDIA3 protein, found in various cell parts, plays key roles in health and disease. This review covers its functions and specific inhibitors, highlighting its potential as a therapeutic target.

Keywords:
CancerCardiovascular systemERp57FertilityInfectionsNervous systemPDI inhibitorsPDIA3PunicalaginVitamin D3

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cell Biology

Background:

  • The protein disulfide isomerase ERp57, also known as PDIA3, is a crucial enzyme involved in protein folding and quality control within the endoplasmic reticulum (ER).
  • ERp57/PDIA3 exhibits diverse subcellular localization, extending beyond the ER to compartments like the nucleus and cell membrane, suggesting multifaceted cellular roles.
  • Its involvement in numerous physiological and pathological processes makes ERp57/PDIA3 a significant target for scientific investigation.

Purpose of the Study:

  • To review and present recent findings on the diverse functions of the ERp57/PDIA3 protein.
  • To summarize newly identified ligands that act as specific inhibitors of PDIA3.
  • To underscore the importance of ERp57/PDIA3 as a research target due to its varied cellular roles and involvement in disease.

Main Methods:

  • Literature review of recent scientific publications on ERp57/PDIA3.
  • Analysis of data regarding the subcellular localization of ERp57/PDIA3.
  • Compilation of information on identified PDIA3-specific inhibitors and their mechanisms.

Main Results:

  • ERp57/PDIA3 is confirmed to be present in multiple cellular locations, including the endoplasmic reticulum, nucleus, and cell membrane.
  • The review details novel functions and physiological/pathological roles associated with ERp57/PDIA3.
  • Several specific inhibitors targeting PDIA3 have been identified and are summarized.

Conclusions:

  • ERp57/PDIA3 is a pleiotropic protein with significant implications across various cellular processes.
  • Understanding the diverse functions and localization of ERp57/PDIA3 is critical for advancing biomedical research.
  • The identified PDIA3-specific inhibitors offer potential avenues for therapeutic development in diseases involving this protein.