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Related Concept Videos

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Export of Misfolded Proteins out of the ER01:32

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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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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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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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Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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CHIP as a membrane-shuttling proteostasis sensor.

Yannick Kopp1,2, Wei-Han Lang1,2, Tobias B Schuster1,2

  • 1Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany.

Elife
|November 2, 2017
PubMed
Summary
This summary is machine-generated.

During cellular stress, the protein CHIP acts as a proteostasis sensor by binding to cell membranes. This allows it to help reorganize cellular compartments, like fragmenting the Golgi apparatus.

Keywords:
cell biologyhumanmembranemolecular chaperonesmouseorganelleproteostasisstress responseubiquitin

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cells adapt to cytosolic protein misfolding via gene transcription and post-transcriptional modifications.
  • Cellular structural changes occur alongside functional responses to stress, but early adaptation mechanisms of compartments are unclear.

Purpose of the Study:

  • To investigate the mechanisms of early cellular compartment adaptation to cytosolic protein misfolding.
  • To elucidate the role of the mammalian ubiquitin ligase C-terminal Hsp70-interacting protein (CHIP) in sensing and responding to cellular stress.

Main Methods:

  • In vitro reconstitution of CHIP-membrane interactions using liposomes.
  • Biochemical assays to determine binding affinities and competition between HSP70 and membranes for CHIP.

Main Results:

  • Chaperone-free CHIP docks on cellular membranes, functioning as a proteostasis sensor.
  • Phosphatidic acid and phosphatidylinositol-4-phosphate promote CHIP association with liposomes.
  • HSP70 and membranes compete for mutually exclusive binding to CHIP's tetratricopeptide repeat domain.

Conclusions:

  • CHIP's relocation to membranes upon stress allows it to sense proteostasis.
  • CHIP can participate in organelle reorganization, demonstrated by Golgi fragmentation.
  • This highlights a novel mechanism for cellular adaptation to proteotoxic stress.