English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Proteomics reveals distinct mechanisms regulating the release of cytokines and alarmins during pyroptosis

Phulphagar, K., Kuehn, L. I., Ebner, S., Frauenstein, A., Swietlik, J. J., Rieckmann, J., et al. (2021). Proteomics reveals distinct mechanisms regulating the release of cytokines and alarmins during pyroptosis. Cell Reports, 34(10): 108826. doi:10.1016/j.celrep.2021.108826.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Phulphagar, Kshiti1, Author              
Kuehn, Lars I.1, Author
Ebner, Stefan1, Author              
Frauenstein, Annika1, Author              
Swietlik, Jonathan J.1, Author              
Rieckmann, Jan1, Author              
Meissner, Felix1, Author              
Affiliations:
1Meissner, Felix / Experimental Systems Immunology, Max Planck Institute of Biochemistry, Max Planck Society, ou_2149678              

Content

show
hide
Free keywords: Q EXACTIVE HF; GASDERMIN-D; UNCONVENTIONAL SECRETION; PORE FORMATION; CELL-DEATH; INFLAMMASOME; MEMBRANE; ACTIVATION; INTERLEUKIN-1-BETA; QUANTIFICATIONCell Biology;
 Abstract: A major pathway for proinflammatory protein release by macrophages is inflammasome-mediated pyroptotic cell death. As conventional secretion, unconventional secretion, and cell death are executed simultaneously, however, the cellular mechanisms regulating this complex paracrine program remain incompletely understood. Here, we devise a quantitative proteomics strategy to define the cellular exit route for each protein by pharmacological and genetic dissection of cellular checkpoints regulating protein release. We report the release of hundreds of proteins during pyroptosis, predominantly due to cell lysis. They comprise constitutively expressed and transcriptionally induced proteins derived from the cytoplasm and specific intracellular organelles. Many low-molecular-weight proteins including the cytokine interleukin-1b, alarmins, and lysosomal-cargo proteins exit cells in the absence of cell lysis. Cytokines and alarmins are released in an endoplasmic reticulum (ER)-Golgi-dependent manner as free proteins rather than by extracellular vesicles. Our work provides an experimental framework for the dissection of cellular exit pathways and a resource for pyroptotic protein release.

Details

show
hide
Language(s): eng - English
 Dates: 2021
 Publication Status: Published online
 Pages: 20
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Cell Reports
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Maryland Heights, MO : Cell Press
Pages: - Volume / Issue: 34 (10) Sequence Number: 108826 Start / End Page: - Identifier: ISSN: 2211-1247
CoNE: https://pure.mpg.de/cone/journals/resource/2211-1247