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A chemical inhibitor of IST1-CHMP1B interaction impairs endosomal recycling and induces noncanonical LC3 lipidation

Knyazeva, Anastasia, 1995- (author)
Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR),Science for Life Laboratory, Umeå University, Umeå, Sweden
Li, Shuang (author)
Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR),Science for Life Laboratory, Umeå University, Umeå, Sweden
Corkery, Dale P. (author)
Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR),Science for Life Laboratory, Umeå University, Umeå, Sweden
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Shankar, Kasturika (author)
Umeå universitet,Umeå Centre for Microbial Research (UCMR),Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM),Molekylär Infektionsmedicin, Sverige (MIMS),Institutionen för medicinsk kemi och biofysik
Herzog, Laura K. (author)
Umeå universitet,Umeå Centre for Microbial Research (UCMR),Institutionen för medicinsk kemi och biofysik,Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM),Molekylär Infektionsmedicin, Sverige (MIMS)
Zhang, Xuepei (author)
Chemical Proteomics Core Facility, Division of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden; Chemical Proteomics Unit, Science for Life Laboratory, Stockholm, Sweden; Chemical Proteomics, Swedish National Infrastructure for Biological Mass Spectrometry, Stockholm, Sweden
Singh, Birendra (author)
Umeå universitet,Anestesiologi och intensivvård
Niggemeyer, Georg (author)
Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany
Grill, David (author)
Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany
Gilthorpe, Jonathan D. (author)
Umeå universitet,Institutionen för integrativ medicinsk biologi (IMB)
Gaetani, Massimiliano (author)
Chemical Proteomics Core Facility, Division of Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden; Chemical Proteomics Unit, Science for Life Laboratory, Stockholm, Sweden; Chemical Proteomics, Swedish National Infrastructure for Biological Mass Spectrometry, Stockholm, Sweden
Carlson, Lars-Anders (author)
Umeå universitet,Umeå Centre for Microbial Research (UCMR),Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM),Molekylär Infektionsmedicin, Sverige (MIMS),Institutionen för medicinsk kemi och biofysik
Waldmann, Herbert (author)
Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany; Faculty of Chemistry and Chemical Biology, Technical University Dortmund, Dortmund, Germany
Wu, Yao-Wen, Professor (author)
Umeå universitet,Kemiska institutionen,Umeå Centre for Microbial Research (UCMR),Science for Life Laboratory, Umeå University, Umeå, Sweden
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 (creator_code:org_t)
Proceedings of the National Academy of Sciences, 2024
2024
English.
In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 121:17
Related links:
https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
https://urn.kb.se/re...
https://doi.org/10.1...
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  • Journal article (peer-reviewed)
Abstract Subject headings
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  • The endosomal sorting complex required for transport (ESCRT) machinery constitutes multisubunit protein complexes that play an essential role in membrane remodeling and trafficking. ESCRTs regulate a wide array of cellular processes, including cytokinetic abscission, cargo sorting into multivesicular bodies (MVBs), membrane repair, and autophagy. Given the versatile functionality of ESCRTs, and the intricate organizational structure of the ESCRT machinery, the targeted modulation of distinct ESCRT complexes is considerably challenging. This study presents a pseudonatural product targeting IST1-CHMP1B within the ESCRT-III complexes. The compound specifically disrupts the interaction between IST1 and CHMP1B, thereby inhibiting the formation of IST1-CHMP1B copolymers essential for normal-topology membrane scission events. While the compound has no impact on cytokinesis, MVB sorting, or biogenesis of extracellular vesicles, it rapidly inhibits transferrin receptor recycling in cells, resulting in the accumulation of transferrin in stalled sorting endosomes. Stalled endosomes become decorated by lipidated LC3, suggesting a link between noncanonical LC3 lipidation and inhibition of the IST1-CHMP1B complex.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Neurovetenskaper (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Neurosciences (hsv//eng)

Keyword

endosomal recycling
ESCRT
IST1-CHMP1B
noncanonical LC3 lipidation
Tantalosin

Publication and Content Type

ref (subject category)
art (subject category)

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