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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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,...
Overview of Transposition and Recombination02:13

Overview of Transposition and Recombination

Transposons make up a significant part of genomes of various organisms. Therefore, it is believed that transposition played a major evolutionary role in speciation by changing genome sizes and modifying gene expression patterns. For example, in bacteria, transposition can lead to conferring antibiotic resistance. Movement of transposable elements within the genetic pool of pathogenic bacteria can aid in transfer of antibiotic-resistant genetic elements. In eukaryotes, transposons can carry out...
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...

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Transient Gene Expression in Tobacco using Gibson Assembly and the Gene Gun
12:02

Transient Gene Expression in Tobacco using Gibson Assembly and the Gene Gun

Published on: April 18, 2014

To translocate or not: that is the problem.

Wayne I Lencer1, Rodney K Tweten

  • 1Department of Medicine, Children's Hospital Boston, Harvard Medical School, MA 02115, USA. wayne.lencer@childrens.harvard.edu

Cell Host & Microbe
|September 20, 2011
PubMed
Summary

Botulinum toxins (BoNTs) enter cells by crossing acidic endosomes. Receptor binding causes pH-dependent changes in BoNTs, enabling cell entry and toxicity.

Area of Science:

  • Cellular Biology
  • Toxicology
  • Molecular Biology

Background:

  • Botulinum toxins (BoNTs) are potent neurotoxins that exert their effects by entering the cytosol of host cells.
  • Entry into the host cell occurs via translocation across the membrane of acidic endosomes, a critical step for cellular toxicity.

Discussion:

  • The mechanism of BoNT entry involves navigating the acidic environment within endosomes.
  • Understanding the conformational changes BoNTs undergo is crucial for elucidating their cellular toxicity pathway.

Key Insights:

  • Sun et al. (2011) demonstrate that BoNT binding to cell surface receptors is a prerequisite for pH-dependent conformational alterations.
  • These conformational changes are essential for the toxin's translocation into the host cell cytosol.

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Studying Membrane Protein Trafficking in Drosophila Photoreceptor Cells Using eGFP-Tagged Proteins

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Determination of the Optimal Chromosomal Location(s) for a DNA Element in Escherichia coli Using a Novel Transposon-mediated Approach
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Determination of the Optimal Chromosomal Location(s) for a DNA Element in Escherichia coli Using a Novel Transposon-mediated Approach

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Studying Membrane Protein Trafficking in Drosophila Photoreceptor Cells Using eGFP-Tagged Proteins

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Determination of the Optimal Chromosomal Location(s) for a DNA Element in Escherichia coli Using a Novel Transposon-mediated Approach
11:12

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  • The study highlights the interplay between receptor engagement and endosomal escape for BoNT activity.

    • Outlook:

    • Further research could explore therapeutic strategies targeting these pH-dependent conformational changes to inhibit BoNT toxicity.
    • Investigating the specific structural dynamics of BoNTs during endosomal escape may reveal new avenues for intervention.
    • This work provides a foundation for understanding toxin-host interactions at the molecular level.