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Videos de Conceptos Relacionados

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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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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Protein Transport to the Stroma01:24

Protein Transport to the Stroma

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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.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
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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.
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,...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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.
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...
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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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Purification of Hsp104, a Protein Disaggregase
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Purification of Hsp104, a Protein Disaggregase

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La proteasa Ste24 limpia los translocos obstruidos

Tslil Ast1, Susan Michaelis2, Maya Schuldiner1

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

Cell
|January 16, 2016
PubMed
Resumen

La metaloproteasa Ste24 del retículo endoplasmático (ER) resuelve la obstrucción del translocón, un estado de translocación de proteínas defectuoso. Este mecanismo de control de calidad de ER se conserva en los seres humanos, salvaguardando la biogénesis de las proteínas.

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Área de la Ciencia:

  • Biología celular
  • Biología molecular
  • Biogénesis de las proteínas

Sus antecedentes:

  • La translocación de proteínas en el retículo endoplasmático (ER) es crucial para la biogénesis de proteínas de la endomembrana.
  • Los mecanismos de control de calidad de ER para resolver errores de translocación, como la obstrucción de translocon, no se comprenden bien.

Objetivo del estudio:

  • Identificar la maquinaria responsable de la resolución de la obstrucción de las translocas.
  • Investigar el papel de la metaloproteasa ER Ste24 en la eliminación de los translocos obstruidos.

Principales métodos:

  • Prueba genética sistemática en Saccharomyces cerevisiae.
  • Ensayos bioquímicos para analizar las interacciones proteína-proteína y la escisión.
  • Análisis funcional del homólogo humano conservado ZMPSTE24.

Principales resultados:

  • La metaloproteasa ER Ste24 fue identificada como un factor clave en la resolución de la obstrucción translocal.
  • Ste24 interactúa con los sustratos de translocación obstruidos y los rompe.
  • El ZMPSTE24 humano realiza funciones conservadas, pero los mutantes asociados a la enfermedad se ven afectados en la eliminación del translocon.

Conclusiones:

  • Ste24 juega un papel crítico en el control de calidad de ER al resolver la obstrucción translocal.
  • Esta función se conserva evolutivamente, destacando su importancia en el mantenimiento de la homeostasis celular.
  • Los defectos en la función ZMPSTE24 pueden contribuir a enfermedades asociadas con errores de translocación de proteínas.