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Related Concept Videos

The Proteasome02:18

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Export of Misfolded Proteins out of the ER01:32

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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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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

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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.
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Related Experiment Video

Updated: May 6, 2026

Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation

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Protease-mediated ectodomain shedding.

Peter Clark

    Thorax
    |November 15, 2013
    PubMed
    Summary
    This summary is machine-generated.

    Ectodomain shedding, the release of protein parts from cell surfaces, is vital in cell communication and survival. Elevated lung protease activity in emphysema may increase this shedding process in lung cells.

    Keywords:
    ADAMsemphysemamatrix metalloproteinasesecretasesheddase

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Medicine

    Background:

    • Ectodomain shedding involves the enzymatic cleavage of cell surface proteins, releasing their extracellular portions.
    • This process plays a critical role in physiological functions such as growth factor signaling, cell adhesion, and survival.
    • Dysregulation of ectodomain shedding is implicated in various pathological conditions.

    Purpose of the Study:

    • To review the key mechanisms and implications of ectodomain shedding.
    • To explore the potential role of enhanced ectodomain shedding in the pathogenesis of emphysema.

    Main Methods:

    • Literature review of ectodomain shedding processes.
    • Analysis of protease activity in lung pathology, specifically emphysema.

    Main Results:

    • Ectodomain shedding is a fundamental biological process with diverse cellular consequences.
    • Increased protease activity, a hallmark of emphysema, is hypothesized to promote ectodomain shedding in lung cells.

    Conclusions:

    • Ectodomain shedding is a significant mechanism in both normal physiology and disease.
    • Further investigation into ectodomain shedding in emphysema could reveal novel therapeutic targets.