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Adekunle T. Bademosi
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Journal Articles
Yong Zhou, Nicholas Ariotti, James Rae, Hong Liang, Vikas Tillu, Shern Tee, Michele Bastiani, Adekunle T. Bademosi, Brett M. Collins, Frederic A. Meunier, John F. Hancock, Robert G. Parton
Journal:
Journal of Cell Biology
Journal of Cell Biology (2021) 220 (3): e202005138.
Published: 26 January 2021
Abstract
Caveolae are specialized domains of the vertebrate cell surface with a well-defined morphology and crucial roles in cell migration and mechanoprotection. Unique compositions of proteins and lipids determine membrane architectures. The precise caveolar lipid profile and the roles of the major caveolar structural proteins, caveolins and cavins, in selectively sorting lipids have not been defined. Here, we used quantitative nanoscale lipid mapping together with molecular dynamic simulations to define the caveolar lipid profile. We show that caveolin-1 (CAV1) and cavin1 individually sort distinct plasma membrane lipids. Intact caveolar structures composed of both CAV1 and cavin1 further generate a unique lipid nano-environment. The caveolar lipid sorting capability includes selectivities for lipid headgroups and acyl chains. Because lipid headgroup metabolism and acyl chain remodeling are tightly regulated, this selective lipid sorting may allow caveolae to act as transit hubs to direct communications among lipid metabolism, vesicular trafficking, and signaling.
Journal Articles
Ravikiran Kasula, Ye Jin Chai, Adekunle T. Bademosi, Callista B. Harper, Rachel S. Gormal, Isabel C. Morrow, Eric Hosy, Brett M. Collins, Daniel Choquet, Andreas Papadopulos, Frédéric A. Meunier
Journal:
Journal of Cell Biology
Journal of Cell Biology (2016) 214 (7): 847–858.
Published: 19 September 2016
Abstract
Munc18-1 and syntaxin-1A control SNARE-dependent neuroexocytosis and are organized in nanodomains on the plasma membrane of neurons and neurosecretory cells. Deciphering the intra- and intermolecular steps via which they prepare secretory vesicles (SVs) for fusion is key to understanding neuronal and hormonal communication. Here, we demonstrate that expression of a priming-deficient mutant lacking 17 residues of the domain 3a hinge-loop (Munc18-1 Δ317-333 ) in PC12 cells engineered to knockdown Munc18-1/2 markedly prolonged SV docking. Single-molecule analysis revealed nonhomogeneous diffusion of Munc18-1 and syntaxin-1A in and out of partially overlapping nanodomains. Whereas Munc18-1 WT mobility increased in response to stimulation, syntaxin-1A became less mobile. These Munc18-1 and syntaxin-1A diffusional switches were blocked by the expression of Munc18-1 Δ317-333 , suggesting that a conformational change in the Munc18-1 hinge-loop controls syntaxin-1A and subsequent SNARE complex assembly. Accordingly, syntaxin-1A confinement was prevented by expression of botulinum neurotoxin type E. The Munc18-1 domain 3a hinge-loop therefore controls syntaxin-1A engagement into SNARE complex formation during priming.
Includes: Supplementary data