- Cellular transport and secretion
- Fetal and Pediatric Neurological Disorders
- Hippo pathway signaling and YAP/TAZ
- Endoplasmic Reticulum Stress and Disease
- Ubiquitin and proteasome pathways
- Neonatal and fetal brain pathology
- Trace Elements in Health
- Computational Drug Discovery Methods
- Retinal Development and Disorders
- Photosynthetic Processes and Mechanisms
- Mitochondrial Function and Pathology
- Enzyme Structure and Function
- Retinopathy of Prematurity Studies
- Protein Structure and Dynamics
- Vestibular and auditory disorders
- Retinal and Macular Surgery
University of Bristol
2018-2023
AstraZeneca (Sweden)
2017
The Commander complex is required for endosomal recycling of diverse transmembrane cargos and mutated in Ritscher-Schinzel syndrome. It comprises two sub-assemblies: Retriever composed VPS35L, VPS26C, VPS29; the CCC which contains twelve subunits: COMMD1-COMMD10 coiled-coil domain-containing (CCDC) proteins CCDC22 CCDC93. Combining X-ray crystallography, electron cryomicroscopy, silico predictions, we have assembled a complete structural model Commander. distantly related to Retromer but has...
The COMMD proteins are a conserved family of with central roles in intracellular membrane trafficking and transcription. They form oligomeric complexes each other act as components larger assembly called the CCC complex, which is localized to endosomal compartments mediates transport several transmembrane cargos. How these formed however completely unknown. Here, we have systematically characterised interactions between human proteins, determined structures using X-ray crystallography...
Evaluating the ligandability of a protein target is key component when defining hit-finding strategies or prioritize among drug targets. Computational as well biophysical approaches based on nuclear magnetic resonance (NMR) fragment screening are powerful but suffer from specific constraints that limit their usage. Here, we demonstrate applicability high-throughput thermal scanning (HTTS) simple and generic method to reproduce assessments NMR-based screening. By applying this large set...
Abstract The sorting nexin SNX17 controls endosome-to-cell surface recycling of diverse transmembrane cargo proteins including integrins, the amyloid precursor protein and lipoprotein receptors. This requires association with multi-subunit Commander trafficking complex, which depends on C-terminus through unknown mechanisms. Using affinity enrichment proteomics, we find that a C-terminal peptide is not only sufficient for interaction but also associates members actin-associated PDZ LIM...
SUMMARY The Commander complex is required for endosomal recycling of diverse transmembrane cargos and mutated in Ritscher-Schinzel syndrome. It comprises two subassemblies; Retriever composed VPS35L, VPS26C VPS29, the CCC which contains ten subunits COMMD1-COMMD10 coiled-coil domain-containing (CCDC) proteins CCDC22 CCDC93. Combining X-ray crystallography, electron cryomicroscopy silico predictions we have assembled a complete structural model Commander. distantly related to Retromer but has...
The Commander complex is required for endosomal recycling of diverse transmembrane cargos and mutated in Ritscher-Schinzel syndrome. It comprises two subassemblies; Retriever composed VPS35L, VPS26C VPS29, the CCC which contains ten subunits COMMD1-COMMD10 coiled-coil domain-containing (CCDC) proteins CCDC22 CCDC93. Combining X-ray crystallography, electron cryomicroscopy silico predictions we have assembled a complete structural model Commander. distantly related to Retromer but has unique...
The sorting nexin SNX17 controls endosome-to-cell surface recycling of diverse transmembrane cargo proteins including integrins, the amyloid precursor protein and lipoprotein receptors. This requires association with multi-subunit Commander trafficking complex, which depends on C-terminus through unknown mechanisms. Using affinity enrichment proteomics, we find that a C-terminal peptide is not only sufficient for interaction but also associates members actin-associated PDZ LIM domain (PDLIM)...