Mitochondrial Membranes Lab
Scientic Supervisor / Contact Person
Name and Surname
Iván López Montero
ORCID (link)
Localization & Research Area
Faculty / Institute
Institute of Multidisciplinary Institute
Department
Physical Chemistry
Research Area
Life Sciences (LIF), Physics (PHY)
MSCA & ERC experience
Research group / research team hosted any MSCA fellow?
Yes
Research group / research team have any ERC beneficiaries?
Yes
Research Team & Research Topic
Research Team / Research Group Name (if any)
Mitochondrial Membranes Lab
Website of the Research team / Research Group / Department
Brief description of the Research Team / Research Group / Department
The mitochondrial membranes lab (MML) is essentially devoted to the reconstitution of fundamental mitochondrial proteins in model membranes with the main goal of understanding and controlling their dynamics and self-assembly under out-of-equilibrium conditions. The MML gathers a broad experience in membrane biophysics and biochemistry of artificial systems. The knowledge is applied for the generation of new bioinspired drug delivery systems and the identification of mitochondrial membranes as a novel therapeutic target against rare diseases. Headed by Iván López Montero, the MML is currently formed by 2 assistant professors, 3 postdoctoral researchers, 3 PhD students and several undergraduate students. The MML is equipped with a wet lab, cell culture (prokaryote and eukaryote), protein purification tools and a wide range of techniques for the mechanical characterization of biomimetic model membranes (confocal microscopy, micromanipulation, surface tension). Our experimental capabilities have been recently expanded to time-resolved fluorescence microscopy (FLIM, FRET, TR-anisotropy, FCS) and High-Speed Atomic Force Microscopy (HS-AFM).
Research lines / projects proposed
The MML is currently focused on:
1. The membrane biophysics of ATP synthase: Investigating the interplay between ATP synthase and lipid membranes. In particular, the ability of rotating ATP synthases for membrane remodeling and protein organization in model systems. Key insights from the lab include the membrane mechanical characterization under active conditions (PNAS 2017; 10.1073/pnas.17012071140) or the active curvature sorting of ATP synthase (Adv Sci 2023, 10.1002/advs.202301606).
2. Mitochondrial Membrane Fusion: Unraveling the molecular mechanisms underlying membrane fusion mediated by mitofusins. Recently, the MML successfully achieved the functional reconstitution of Mitofusin 2 (Mfn2) in giant vesicles (PNAS 2024, 10.1073/pnas.231360912), paving the way for new research directions into molecular interactions and regulatory mechanisms.
3. Membrane Reconstitution of OXPHOS Proteins: The MML has recently contributed to the reconstitution of mitochondrial Complex I into proteoliposomes, demonstrating its Na⁺/H⁺ antiporter activity (Cell 2024, 10.1016/j.cell.2024.08.045). Building on this expertise, we aim to extend our studies to other respiratory complexes, such as Complex III, and explore the co-reconstitution of multiple complexes for artificial realizations and fundamental investigations into protein-membrane interactions.
1. The membrane biophysics of ATP synthase: Investigating the interplay between ATP synthase and lipid membranes. In particular, the ability of rotating ATP synthases for membrane remodeling and protein organization in model systems. Key insights from the lab include the membrane mechanical characterization under active conditions (PNAS 2017; 10.1073/pnas.17012071140) or the active curvature sorting of ATP synthase (Adv Sci 2023, 10.1002/advs.202301606).
2. Mitochondrial Membrane Fusion: Unraveling the molecular mechanisms underlying membrane fusion mediated by mitofusins. Recently, the MML successfully achieved the functional reconstitution of Mitofusin 2 (Mfn2) in giant vesicles (PNAS 2024, 10.1073/pnas.231360912), paving the way for new research directions into molecular interactions and regulatory mechanisms.
3. Membrane Reconstitution of OXPHOS Proteins: The MML has recently contributed to the reconstitution of mitochondrial Complex I into proteoliposomes, demonstrating its Na⁺/H⁺ antiporter activity (Cell 2024, 10.1016/j.cell.2024.08.045). Building on this expertise, we aim to extend our studies to other respiratory complexes, such as Complex III, and explore the co-reconstitution of multiple complexes for artificial realizations and fundamental investigations into protein-membrane interactions.
Key words
Application requirements
Professional Experience & Documents
Applicants must submit a short CV including an early achievements track-record and a motivation letter.
One Page Proposal
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