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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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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.
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...
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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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Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
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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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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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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.
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The Protease Ste24 Clears Clogged Translocons.

Tslil Ast1, Susan Michaelis2, Maya Schuldiner1

  • 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.

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|January 16, 2016
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Summary
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The endoplasmic reticulum (ER) metalloprotease Ste24 resolves translocon clogging, a faulty protein translocation state. This ER quality control mechanism is conserved in humans, safeguarding protein biogenesis.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Biogenesis

Background:

  • Protein translocation into the endoplasmic reticulum (ER) is crucial for endomembrane protein biogenesis.
  • ER quality control mechanisms for resolving translocation errors, such as translocon clogging, are not well understood.

Purpose of the Study:

  • To identify the machinery responsible for resolving translocon clogging.
  • To investigate the role of the ER metalloprotease Ste24 in clearing obstructed translocons.

Main Methods:

  • Systematic genetic screen in Saccharomyces cerevisiae.
  • Biochemical assays to analyze protein-protein interactions and cleavage.
  • Functional analysis of conserved human homolog ZMPSTE24.

Main Results:

  • The ER metalloprotease Ste24 was identified as a key factor in resolving translocon clogging.
  • Ste24 interacts with and cleaves clogged translocation substrates.
  • Human ZMPSTE24 performs conserved functions, but disease-associated mutants are impaired in clearing the translocon.

Conclusions:

  • Ste24 plays a critical role in ER quality control by resolving translocon clogging.
  • This function is evolutionarily conserved, highlighting its importance in maintaining cellular homeostasis.
  • Defects in ZMPSTE24 function may contribute to diseases associated with protein translocation errors.