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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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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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RNA interference (RNAi) is a cellular mechanism that inhibits gene expression by suppressing its transcription or activating the RNA degradation process. The mechanism was discovered by Andrew Fire and Craig Mello in 1998 in plants. Today, it is observed in almost all eukaryotes, including protozoa, flies, nematodes, insects, parasites, and mammals. This precise cellular mechanism of gene silencing has been developed into a technique that provides an efficient way to identify and determine the...
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Dynamic Modulation of IRE1α-XBP1 Signaling by Adenovirus.

Yumi Jang1,2, Fred Bunz1

  • 1Department of Radiation Oncology and Molecular Radiation Sciences, The Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.

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Summary
This summary is machine-generated.

Adenovirus serotype 5 (HAdV5) manipulates the unfolded protein response (UPR) by activating IRE1α but blocking XBP1s production. This viral strategy evades host defenses, highlighting complex UPR control during infection.

Keywords:
XBP1 splicingadenovirusp53unfolded protein response

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Area of Science:

  • Cellular stress responses
  • Virology
  • Molecular biology

Background:

  • Viral infections trigger host cell stress responses, including the unfolded protein response (UPR).
  • The UPR aims to restore protein homeostasis, involving signaling pathways like inositol-requiring enzyme type 1 (IRE1α) and X-box binding protein 1 (XBP1).
  • Adenovirus serotype 5 (HAdV5) is known to activate the UPR, with prior studies suggesting IRE1α-XBP1 activity aids viral replication.

Purpose of the Study:

  • To investigate the precise mechanisms by which HAdV5 interacts with the IRE1α-XBP1 axis of the UPR.
  • To elucidate the opposing effects of HAdV5 on IRE1α activation and XBP1s production.
  • To understand the role of the tumor suppressor p53 in modulating the UPR during HAdV5 infection.

Main Methods:

  • Analysis of IRE1α activation and XBP1s production in HAdV5-infected cells.
  • Investigating the impact of HAdV5-mediated p53 degradation on IRE1α signaling.
  • Utilizing molecular biology techniques to study UPR pathway modulation.

Main Results:

  • HAdV5 activates IRE1α but simultaneously blocks the post-transcriptional production of the XBP1s isoform.
  • The tumor suppressor p53 inhibits IRE1α activation, and its degradation by HAdV5 leads to IRE1α de-repression.
  • HAdV5 co-opts IRE1α signaling while suppressing XBP1s, indicating a complex viral evasion strategy.

Conclusions:

  • HAdV5 employs opposing strategies to control the UPR, activating IRE1α while inhibiting XBP1s.
  • The interplay between p53, IRE1α, and XBP1s represents a critical battleground for cell fate during HAdV5 infection.
  • Understanding these viral manipulation mechanisms provides insights into host-pathogen interactions and UPR regulation.