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Related Concept Videos

Energy to Drive Translocation01:37

Energy to Drive Translocation

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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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Mitochondrial Precursor Proteins01:39

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Translocation of Proteins into the Mitochondria01:19

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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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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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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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The Unfolded Protein Response01:37

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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
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Related Experiment Video

Updated: Jul 16, 2025

RNA Interference-based Investigation of the Function of Heat Shock Protein 27 during Corneal Epithelial Wound Healing
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RNA Interference-based Investigation of the Function of Heat Shock Protein 27 during Corneal Epithelial Wound Healing

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The heat shock protein Hsp27 controls mitochondrial function by modulating ceramide generation.

Rowan A Boyd1, Saurav Majumder1, Johnny Stiban2

  • 1Department of Biochemistry and Molecular Biology, Virginia Commonwealth University School of Medicine, Richmond, VA 23398, USA.

Cell Reports
|September 9, 2023
PubMed
Summary

Heat shock protein 27 (Hsp27) inhibits ceramide synthase 1 (CerS1), impacting cellular signaling and mitochondrial function. This protein interaction regulates ceramide levels and mitophagy, crucial for cellular health.

Keywords:
C18-ceramideCP: Molecular biologyCerS1Hsp27ceramideceramide synthasemitophagysphingolipids

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Related Experiment Videos

Last Updated: Jul 16, 2025

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Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Sphingolipids are vital for cell membrane structure and signaling.
  • Ceramide, central to sphingolipid metabolism, is synthesized by ceramide synthases (CerS).
  • Regulatory mechanisms for CerS enzymes remain largely uncharacterized.

Purpose of the Study:

  • To identify novel regulators of ceramide synthases (CerS).
  • To elucidate the functional role of protein-protein interactions in CerS regulation.
  • To investigate the impact of CerS regulation on cellular processes like mitophagy.

Main Methods:

  • Unbiased proteomics approach to identify interacting proteins.
  • In vitro and cellular assays to assess enzyme activity and protein binding.
  • Gene silencing and mutagenesis to study functional consequences.
  • Mitochondrial function assays and mitophagy assessment.

Main Results:

  • Small heat shock protein 27 (Hsp27) specifically interacts with Ceramide Synthase 1 (CerS1).
  • Hsp27 acts as an endogenous inhibitor of CerS1 activity; Hsp27 binding is crucial for inhibition.
  • Hsp27 knockdown increases cellular ceramide levels and impairs mitochondrial function, inducing mitophagy via CerS1.
  • Hsp27 phosphorylation modulates its interaction with CerS1 and enzyme activity during stress.

Conclusions:

  • Hsp27 is identified as a novel, specific regulator of CerS1.
  • The Hsp27-CerS1 interaction provides a new mechanism for controlling ceramide homeostasis.
  • Hsp27-mediated regulation of CerS1 plays a critical role in managing mitochondrial function and mitophagy.