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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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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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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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The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

7.6K
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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Nervous Tissue: Myelin01:25

Nervous Tissue: Myelin

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The myelin sheath is a multilayered lipid and protein covering that insulates the axon of a neuron, enhancing the speed of nerve impulse conduction. Axons without this sheath are referred to as unmyelinated. Two types of neuroglia, Schwann cells in the peripheral nervous system (PNS) and oligodendrocytes in the central nervous system (CNS) are responsible for producing myelin sheaths.
Schwann cells begin to form myelin sheaths around axons during fetal development. They wrap around a small...
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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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Comprehensive Autopsy Program for Individuals with Multiple Sclerosis
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Endoplasmic reticulum quality control and dysmyelination.

Allison Kraus, Marek Michalak

    Biomolecular Concepts
    |May 12, 2015
    PubMed
    Summary

    Dysmyelination, linked to neurological diseases, stems from endoplasmic reticulum dysfunction. This organelle is crucial for myelin health and its molecular machinery impacts myelin pathologies.

    Area of Science:

    • Neuroscience
    • Cell Biology
    • Biochemistry

    Background:

    • Dysmyelination underlies severe neurological disorders like multiple sclerosis and schizophrenia.
    • Intact myelin sheaths are essential for neuronal health and proper nerve signal transmission.
    • Endoplasmic reticulum (ER) dysfunction is increasingly recognized as a root cause of myelin defects.

    Purpose of the Study:

    • To review the critical role of the endoplasmic reticulum in myelin formation and maintenance.
    • To highlight how ER resident molecules contribute to myelin pathologies.
    • To underscore the ER as a key upstream regulator of myelin homeostasis.

    Main Methods:

    • Literature review of studies investigating myelin biology and endoplasmic reticulum function.
    • Analysis of molecular mechanisms linking ER stress and protein quality control to myelin defects.

    More Related Videos

    Preparation of Rat Oligodendrocyte Progenitor Cultures and Quantification of Oligodendrogenesis Using Dual-infrared Fluorescence Scanning
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    Preparation and Immunostaining of Myelinating Organotypic Cerebellar Slice Cultures
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    Preparation of Rat Oligodendrocyte Progenitor Cultures and Quantification of Oligodendrogenesis Using Dual-infrared Fluorescence Scanning
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    Preparation and Immunostaining of Myelinating Organotypic Cerebellar Slice Cultures
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  • Synthesis of findings on ER's role in cholesterol biosynthesis and calcium homeostasis in myelin.

    • Main Results:

    • The ER is central to myelin protein folding, quality control, and lipid biosynthesis.
    • ER stress and impaired calcium regulation directly impact myelin sheath integrity.
    • Dysfunctional ER molecular pathways are implicated in diverse dysmyelinating diseases.

    Conclusions:

    • The endoplasmic reticulum is a dynamic and pivotal organelle in myelin development and disease.
    • Targeting ER resident molecules offers potential therapeutic strategies for dysmyelinating conditions.
    • Understanding ER-myelin interactions is key to addressing neurological disabilities caused by myelin damage.