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Related Concept Videos

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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Energy to Drive Translocation01:37

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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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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Nuclear Export01:42

Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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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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Related Experiment Video

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Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
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Extracellular Hsp70: export and function.

Antonio De Maio1

  • 1University of California San Diego, 9500 Gilman Drive, #0739, La Jolla, CA 92093-0739, USA. ademaio@ucsd.edu.

Current Protein & Peptide Science
|April 4, 2014
PubMed
Summary

Heat shock proteins (HSPs) are released outside cells, acting as stress signals for immune cells. This review explores extracellular HSP functions and release mechanisms, focusing on Hsp70.

Area of Science:

  • Cellular stress response
  • Molecular biology
  • Immunology

Background:

  • Heat shock proteins (HSPs) are crucial for cellular repair after stress.
  • Traditionally, HSPs were thought to function solely intracellularly.
  • Emerging evidence shows extracellular HSPs have distinct signaling roles.

Purpose of the Study:

  • To review the functions of extracellular heat shock proteins.
  • To explore proposed mechanisms for HSP export from cells.
  • To highlight the role of extracellular Hsp70.

Main Methods:

  • Literature review of cellular stress response and HSP research.
  • Analysis of proposed mechanisms for extracellular HSP release.
  • Focus on Hsp70 as a key inducible extracellular HSP.

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Intracellular Refolding Assay
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Intracellular Refolding Assay
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Main Results:

  • Extracellular HSPs function as alert signals, particularly for the immune system.
  • Multiple release pathways exist, including vesicle-associated and passive release.
  • Extracellular HSPs can be membrane-bound or free, associated with client proteins or not.

Conclusions:

  • Extracellular HSPs play a critical role in intercellular communication and immune priming.
  • Understanding HSP export mechanisms is key to their extracellular function.
  • Hsp70 is a significant player in extracellular stress signaling.