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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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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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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Protein Transport to the Outer Chloroplast Membrane01:11

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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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Cotranslational Protein Translocation01:20

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Related Experiment Video

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Leaky endosomes push tau over the seed limit.

Chris Ugbode1, Laura Fort-Aznar1, Sean T Sweeney2

  • 1Department of Biology, University of York, York YO10 5DD, United Kingdom.

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Researchers identified key cellular machinery involved in the spread of tau protein aggregates, a hallmark of neurodegenerative diseases. Maintaining endolysosomal function is crucial for preventing this intracellular propagation.

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Area of Science:

  • Neurobiology
  • Cell Biology
  • Genetics

Background:

  • Protein aggregation, particularly of tau, is implicated in neurodegenerative disease progression.
  • The mechanisms governing the spread of tau aggregates within and between cells remain poorly understood.

Purpose of the Study:

  • To identify cellular components mediating the intracellular propagation of tau aggregates.
  • To elucidate the role of the endosomal sorting complex required for transport (ESCRT) machinery in tau pathology.

Main Methods:

  • Development of a cell-based model for studying tau aggregation.
  • Utilized CRISPR interference (CRISPRi) genetic screening to identify key genes.
  • Investigated the function of ESCRT components in tau aggregate propagation.

Main Results:

  • Identified components of the ESCRT machinery as critical mediators of intracellular tau aggregate spread.
  • Demonstrated that disruption of endolysosomal integrity facilitates tau propagation.
  • Highlighted the role of endolysosomal pathways in controlling tau pathology.

Conclusions:

  • The ESCRT machinery plays a significant role in the intracellular propagation of tau aggregates.
  • Endolysosomal integrity is essential for limiting the spread of tau pathology.
  • These findings offer potential therapeutic targets for neurodegenerative diseases.