Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process

Autor: Monika Słomińska-Wojewódzka, Jowita Nowakowska-Gołacka, Hanna Sominka, Natalia Sowa-Rogozińska
Jazyk: angličtina
Rok vydání: 2019
Předmět:
0301 basic medicine
Proteasome Endopeptidase Complex
Protein Folding
Toxin transport
Review
macromolecular substances
Endoplasmic-reticulum-associated protein degradation
Protein degradation
Endoplasmic Reticulum
Catalysis
Inorganic Chemistry
lcsh:Chemistry
03 medical and health sciences
Cytosol
AB-toxins
AB toxin
Humans
Physical and Theoretical Chemistry
Molecular Biology
lcsh:QH301-705.5
Spectroscopy
Toxins
Biological
030102 biochemistry & molecular biology
Chemistry
Endoplasmic reticulum
Organic Chemistry
Ubiquitination
Endoplasmic Reticulum-Associated Degradation
General Medicine
Computer Science Applications
Cell biology
endoplasmic reticulum (ER)
ER-associated degradation (ERAD)
Vesicular transport protein
Protein Transport
030104 developmental biology
Proteasome
lcsh:Biology (General)
lcsh:QD1-999
Proteolysis
Zdroj: International Journal of Molecular Sciences, Vol 20, Iss 6, p 1307 (2019)
International Journal of Molecular Sciences
ISSN: 1422-0067
Popis: Several bacterial and plant AB-toxins are delivered by retrograde vesicular transport to the endoplasmic reticulum (ER), where the enzymatically active A subunit is disassembled from the holotoxin and transported to the cytosol. In this process, toxins subvert the ER-associated degradation (ERAD) pathway. ERAD is an important part of cellular regulatory mechanism that targets misfolded proteins to the ER channels, prior to their retrotranslocation to the cytosol, ubiquitination and subsequent degradation by a protein-degrading complex, the proteasome. In this article, we present an overview of current understanding of the ERAD-dependent transport of AB-toxins to the cytosol. We describe important components of ERAD and discuss their significance for toxin transport. Toxin recognition and disassembly in the ER, transport through ER translocons and finally cytosolic events that instead of overall proteasomal degradation provide proper folding and cytotoxic activity of AB-toxins are discussed as well. We also comment on recent reports presenting medical applications for toxin transport through the ER channels.
Databáze: OpenAIRE
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