A new quinoline-based chemical probe inhibits the autophagy-related cysteine protease ATG4B View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

D. Bosc, L. Vezenkov, S. Bortnik, J. An, J. Xu, C. Choutka, A. M. Hannigan, S. Kovacic, S. Loo, P. G. K. Clark, G. Chen, R. N. Guay-Ross, K. Yang, W. H. Dragowska, F. Zhang, N. E. Go, A. Leung, N. S. Honson, T. A. Pfeifer, M. Gleave, M. Bally, S. J. Jones, S. M. Gorski, R. N. Young

ABSTRACT

The cysteine protease ATG4B is a key component of the autophagy machinery, acting to proteolytically prime and recycle its substrate MAP1LC3B. The roles of ATG4B in cancer and other diseases appear to be context dependent but are still not well understood. To help further explore ATG4B functions and potential therapeutic applications, we employed a chemical biology approach to identify ATG4B inhibitors. Here, we describe the discovery of 4-28, a styrylquinoline identified by a combined computational modeling, in silico screening, high content cell-based screening and biochemical assay approach. A structure-activity relationship study led to the development of a more stable and potent compound LV-320. We demonstrated that LV-320 inhibits ATG4B enzymatic activity, blocks autophagic flux in cells, and is stable, non-toxic and active in vivo. These findings suggest that LV-320 will serve as a relevant chemical tool to study the various roles of ATG4B in cancer and other contexts. More... »

PAGES

11653

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-018-29900-x

DOI

http://dx.doi.org/10.1038/s41598-018-29900-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1105917951

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30076329


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443 Institut des Biomolécules Max Mousseron (IBMM), UMR 5247 CNRS, Université de Montpellier, ENSCM, Faculté de Pharmacie, 15 avenue Charles Flahault, 34093, Montpellier, France
444 rdf:type schema:Organization
445 https://www.grid.ac/institutes/grid.61971.38 schema:alternateName Simon Fraser University
446 schema:name Canada’s Michael Smith Genome Sciences Centre, BC Cancer Agency, V5Z 4E6, Vancouver, BC, Canada
447 Department of Chemistry, Simon Fraser University, V5A 1S6, Burnaby, BC, Canada
448 Department of Molecular Biology and Biochemistry, Simon Fraser University, V5A 1S6, Burnaby, BC, Canada
449 Inserm, Institut Pasteur de Lille, U1177 Drugs & Molecules for Living Systems, Université de Lille, F-59000, Lille, France
450 Interdisciplinary Oncology Program, University of British Columbia, Vancouver, Canada
451 rdf:type schema:Organization
 




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