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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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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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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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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Tyramide Signal Amplification for the Immunofluorescent Staining of ZBP1-Dependent Phosphorylation of RIPK3 and MLKL After HSV-1 Infection in Human Cells
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14-3-3 and erlin proteins differentially interact with RIPK2 complexes.

Heidrun Steinle1, Kornelia Ellwanger1, Nora Mirza1

  • 1Department of Immunology, Institute of Nutritional Medicine, University of Hohenheim, 70619 Stuttgart, Germany.

Journal of Cell Science
|June 21, 2021
PubMed
Summary

Receptor interacting serine/threonine kinase 2 (RIPK2) forms complexes with erlin-1 and erlin-2 during innate immune signaling. These interactions are specific to certain activation pathways, suggesting a role in cellular responses.

Keywords:
Bacterial infectionErlin-1Erlin-2Innate immunityNod-like receptorsRIP2RIPosome

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Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Signaling

Background:

  • Receptor interacting serine/threonine kinase 2 (RIPK2) is crucial for NOD1 and NOD2 pattern recognition receptor signaling.
  • Activation of NOD1/2 receptors leads to the formation of RIPK2-containing cytoplasmic complexes.
  • Understanding the molecular composition of these complexes is key to elucidating innate immune pathways.

Purpose of the Study:

  • To identify the molecular components of RIPK2-mediated signaling complexes.
  • To investigate the dynamic interactions of RIPK2 with cellular proteins upon NOD1/2 activation.
  • To determine the specificity of protein recruitment to RIPK2 complexes under different activation conditions.

Main Methods:

  • Utilized Shigella flexneri infection to activate NOD1-RIPK2 signaling.
  • Employed protein binding assays and immunofluorescence staining to validate interactions.
  • Investigated RIPK2 complex formation following XIAP depletion and RIPK2 inhibitor treatment.

Main Results:

  • RIPK2 formed dynamic interactions with A20, erlin-1, erlin-2, and 14-3-3 proteins upon Shigella infection.
  • Erlin-1 and erlin-2 (erlin-1/2) specifically bound to RIPK2 complexes, while 14-3-3 interaction decreased.
  • Erlin-1/2 were recruited to RIPK2 complexes after XIAP inhibition but not with RIPK2 inhibitors.

Conclusions:

  • Erlin-1/2 specifically associate with RIPK2 complexes, indicating a potential role in innate immune signaling.
  • The distinct recruitment patterns of erlin-1/2 suggest pathway-specific functions in RIPK2 signaling.
  • Further research is needed to define the biological outcomes of the erlin-1/2-RIPK2 association.