Fernando L. Noguera-Cañas
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Fernando L. Noguera-Cañas has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
Aitor Díaz-Agustín
Instituto de Química Médica (IQM-CSIC), Juan de la Cierva 3, 28006 Madrid, Spain
1 shared publication- Angel Orte
Unidad de Excelencia de Química Aplicada a la Biomedicina y Medioambiente (UEQ) Faculty of Sciences University of Granada Granada Spain
1 shared publication - Francisco Conejero-Lara
Departamento de Química Física, Instituto de Biotecnología e Unidad de Excelencia de Química Aplicada a Biomedicina y Medioambiente (UEQ), Facultad de Ciencias, Universidad de Granada, 18071 Granada, Spain
1 shared publication - Jose Antonio Gavira
Instituto Andaluz de Ciencias de la Tierra
1 shared publication - Jose Manuel Paredes
University of Granada
1 shared publication - Mercedes Martín-Martínez
Instituto de Química Médica (IQM-CSIC), Juan de la Cierva 3, 28006 Madrid, Spain
1 shared publication
Latest Publications
- Open Access
The WIPI homolog Atg18 binds to and tethers membranes containing phosphatidylinositol-3,4,5-triphosphate
Atg18 —for Autophagy-related gene 18— is a member of the PROPPIN (β- prop ellers that bind p olyphospho in ositides) family, which is known for its binding to phosphorylated phosphoinositides through two conserved binding sites. Although Atg18 binding to polyphosphoinositides is crucial for its roles in both autophagic and non-autophagic functions within cells, the precise molecular mechanism by which Atg18 selectively binds to specific phosphatidylinositols remains unresolved. Here, we combined molecular dynamic simulations and biophysical methods —including isothermal titration calorimetry (ITC), cosedimentation, fluorescence resonance energy transfer (FRET), and dynamic light scattering (DLS)— to characterize the interaction between Atg18 and polyphosphoinositides. In contrast to previous findings, we demonstrate that Atg18 binds to and clusters liposomes containing phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P 3 ), suggesting that Atg18 oligomerizes and tethers opposing membranes containing this physiological phosphatidylinositol. Hence, our results provide new insights into how Atg18 and its mammalian homologs, WIPI —for WD-repeat domain phosphoinositide-interacting— proteins, may regulate organelle membrane organization and vesicle trafficking required for both autophagic and non-autophagic functions.
Open AccessThe WIPI homolog Atg18 binds to and tethers membranes containing phosphatidylinositol-3,4,5-triphosphate
Atg18 —for Autophagy-related gene 18— is a member of the PROPPIN (β- prop ellers that bind p olyphospho in ositides) family, which is known for its binding to phosphorylated phosphoinositides through two conserved binding sites. Although Atg18 binding to polyphosphoinositides is crucial for its roles in both autophagic and non-autophagic functions within cells, the precise molecular mechanism by which Atg18 selectively binds to specific phosphatidylinositols remains unresolved. Here, we combined molecular dynamic simulations and biophysical methods —including isothermal titration calorimetry (ITC), cosedimentation, fluorescence resonance energy transfer (FRET), and dynamic light scattering (DLS)— to characterize the interaction between Atg18 and polyphosphoinositides. In contrast to previous findings, we demonstrate that Atg18 binds to and clusters liposomes containing phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P 3 ), suggesting that Atg18 oligomerizes and tethers opposing membranes containing this physiological phosphatidylinositol. Hence, our results provide new insights into how Atg18 and its mammalian homologs, WIPI —for WD-repeat domain phosphoinositide-interacting— proteins, may regulate organelle membrane organization and vesicle trafficking required for both autophagic and non-autophagic functions.