Dr. Walid Houry

The inaugural Proteostasis Researchers in Canada (PRinCE) symposium

3 July 2019|

The Proteostasis Researchers in Canada (PRinCE) inaugural meeting was held at the University of Toronto on June 10-11, 2019. The aim of this first symposium was to establish a network of researchers working in the field of protein homeostasis in Canada and to promote collaborations between labs working on topics relevant to proteostasis. These include (but are not limited to) protein folding, protein trafficking, protein degradation, and neurodegenerative diseases – […]

Structure of human mitochondrial ClpP protease – drug complex gains cover of Cancer Cell

24 May 2019|

The crystal structure of ClpP protease activated by the experimental Phase 2 anti-cancer drug ONC 201, as determined by graduate student Ondrej Halgas in Emil F. Pai’s lab, was featured on the cover of the current issue (May 13th, 2019) of the journal Cancer Cell. Together with the laboratories of Walid Houry, Aaron Schimmer (Medical Biophysics) and Michael Andreeff (MD Anderson, Texas), they identified ClpP as the […]

Dysregulation of the human mitochondrial protease ClpP induces cancer cell death

4 July 2018|

Acyldepsipeptides (ADEPs) compounds have bactericidal properties via dysregulating the activity of the highly conserved tetradecameric bacterial ClpP protease. In a recent publication in Cell Chemical Biology, Keith S. Wong and co-authors from the Houry group have reported on the identification of ADEP analogs that are potent dysregulators of the human mitochondrial ClpP (HsClpP). These analogs interact with HsClpP at high affinity, causing the protease to non-specifically degrade model […]

Mapping the molecular chaperone network

4 October 2017|

Rizzolo et al. from the Houry group provided a comprehensive view of molecular chaperone function in the cell through the use of a systematic global integrative network approach based on physical (protein-protein) and genetic (gene-gene or epistatic) interaction mapping. The analysis revealed the presence of a large chaperone functional supercomplex, which was named the NAJ chaperone complex, encompassing Hsp40, Hsp70, Hsp90, CCT and small Hsps. Many chaperones were found […]

Houry lab identifies a novel regulator of respiratory chain complexes

13 February 2017|

Graphical abstract_120616

An interaction between the respiratory enzyme fumarate reductase (Frd, also known as Complex II) and an ATPase has been identified in E. coli by the Houry lab. The research shows that the RavA ATPase, belonging to a poorly characterized but ubiquitous MoxR family of AAA+ ATPases, associates with the Frd respiratory enzyme through an adaptor, which the group named ViaA. […]