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Related Concept Videos

Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

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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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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Peroxisomes01:24

Peroxisomes

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Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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Ribosome-binding protein 1 maintains peroxisome biogenesis.

Kaneez Fatima1, Helena Vihinen2, Ani Akpinar1

  • 1Institute of Biotechnology , Helsinki Institute of Life Science (HiLIFE), University of Helsinki, 00014 Helsinki, Finland.

Journal of Cell Science
|December 18, 2025
PubMed
Summary
This summary is machine-generated.

Ribosome-binding protein 1 (RRBP1) is a newly discovered factor promoting peroxisome biogenesis in human cells. Its absence leads to fewer peroxisomes and impaired protein processing, but does not affect cell growth.

Keywords:
CRISPR/Cas9PeroxisomePeroxisome biogenesisRRBP1

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Area of Science:

  • Cell Biology
  • Organelle Biogenesis
  • Human Health

Background:

  • Peroxisomes are vital single-membrane organelles crucial for human health.
  • The intricate mechanisms governing peroxisome biogenesis remain incompletely understood.
  • Identifying novel factors involved in peroxisome formation is essential for understanding cellular function.

Purpose of the Study:

  • To identify novel factors regulating peroxisome biogenesis using a systematic screening approach.
  • To elucidate the specific role of the identified factor, ribosome-binding protein 1 (RRBP1), in human cells.
  • To investigate the consequences of RRBP1 depletion on peroxisome number, protein levels, and processing.

Main Methods:

  • Systematic double screening approach to identify peroxisome biogenesis factors.
  • Genetic manipulation (deletion/depletion) of RRBP1 in HEK293T human cells.
  • Analysis of peroxisome number, peroxisomal protein levels, protein processing, cell proliferation, and protein translation.
  • Investigation of peroxisome-endoplasmic reticulum (ER) contact sites and pexophagy.

Main Results:

  • Ribosome-binding protein 1 (RRBP1) was identified as a novel peroxisome biogenesis factor.
  • RRBP1 deletion reduced peroxisome number and peroxisomal protein levels.
  • Defects in processing of peroxisomal matrix proteins (e.g., ACOX1, thiolase) were observed in RRBP1-deficient cells.
  • RRBP1 depletion did not impact cell proliferation, protein translation, peroxisome-ER contact sites, or pexophagy.
  • Absence of RRBP1 led to proteasomal degradation of peroxisomal proteins, indicating a role in protein insertion and stabilization.

Conclusions:

  • RRBP1 plays a significant role in promoting peroxisome biogenesis in human cells.
  • The study highlights the utility of systematic screening methods for discovering novel organellar biogenesis factors.
  • RRBP1 appears to be involved in the membrane insertion and stabilization of peroxisomal proteins.