Resolving the kinetics of lipid, protein and peptide diffusion in membranes

Sanderson, John M.

doi:10.3109/09687688.2012.678018

Cited by 33 publications

(24 citation statements)

References 211 publications

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“…in the order of those observed for membrane-associated proteins [62]. This consideration takes into account experimental and theoretical results showing that motor mobility within the membrane affect transport properties [63,64].…”

Section: Resultsmentioning

confidence: 99%

Mechanical coupling of microtubule-dependent motor teams during peroxisome transport in Drosophila S2 cells

Rossi

Wetzler

Benseñor

et al. 2017

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background Intracellular transport requires molecular motors that step along cytoskeletal filaments actively dragging cargoes through the crowded cytoplasm. Here, we explore the interplay of the opposed polarity motors kinesin-1 and cytoplasmic dynein during peroxisome transport along microtubules in Drosophila S2 cells. Methods We used single particle tracking with nanometer accuracy and millisecond time resolution to extract quantitative information on the bidirectional motion of organelles. The transport performance was studied in cells expressing a slow chimeric plus-end directed motor or the kinesin heavy chain. We also analyzed the influence of peroxisomes membrane fluidity in methyl-β-ciclodextrin treated cells. The experimental data was also confronted with numerical simulations of two well-established tug of war scenarios. Results and conclusions The velocity distributions of retrograde and anterograde peroxisomes showed a multi-modal pattern suggesting that multiple motor teams drive transport in either direction. The chimeric motors interfered with the performance of anterograde transport and also reduced the speed of the slowest retrograde team. In addition, increasing the fluidity of peroxisomes membrane decreased the speed of the slowest ante-rograde and retrograde teams. General significance Our results support the existence of a crosstalk between opposed-polarity motor teams. Moreover, the slowest teams seem to mechanically communicate with each other through the membrane to trigger transport.

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Section: Resultsmentioning

confidence: 99%

Mechanical coupling of microtubule-dependent motor teams during peroxisome transport in Drosophila S2 cells

Rossi

Wetzler

Benseñor

et al. 2017

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…In fact, variations in diffusion coefficients of ≥2 orders of magnitude are a result of the different time scales measured by experiments. 3 , 4 Quasi-elastic neutron scattering measures diffusion on the picosecond time scale, while, for instance, fluorescence correlation spectroscopy (FCS) and fluorescence recovery after photobleaching (FRAP) measure diffusion on longer time scales, showing signatures of Brownian motion. However, a detailed picture of the lateral motion of molecules in a mixed bilayer with cholesterol is still lacking.…”

Section: Introductionmentioning

confidence: 99%

Dynamics of Lipids, Cholesterol, and Transmembrane α-Helices from Microsecond Molecular Dynamics Simulations

Baker

Abrams

2014

J. Phys. Chem. B

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Extensive all-atom molecular dynamics (∼24 μs total) allowed exploration of configurational space and calculation of lateral diffusion coefficients of the components of a protein-embedded, cholesterol-containing model bilayer. The three model membranes are composed of an ∼50/50 (by mole) dipalmitoylphosphatidylcholine (DPPC)/cholesterol bilayer and contained an α-helical transmembrane protein (HIV-1 gp41 TM). Despite the high concentration of cholesterol, normal Brownian motion was observed and the calculated diffusion coefficients (on the order of 10–9 cm2/s) are consistent with experiments. Diffusion is sensitive to a variety of parameters, and a temperature difference of ∼4 K from thermostat artifacts resulted in 2–10-fold differences in diffusion coefficients and significant differences in lipid order, membrane thickness, and unit cell area. Also, the specific peptide sequence likely underlies the consistently observed faster diffusion in one leaflet. Although the simulations here present molecular dynamics (MD) an order of magnitude longer than those from previous studies, the three systems did not approach ergodicity. The distributions of cholesterol and DPPC around the peptides changed on the microsecond time scale, but not significantly enough to thoroughly explore configurational space. These simulations support conclusions of other recent microsecond MD in that even longer time scales are needed for equilibration of model membranes and simulations of more realistic cellular or viral bilayers.

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“…Although it has since become clear that cell membranes are extremely diverse, dynamic and complex structures, 2 this notion of chemical inertness has remained unchallenged. Diacylphospholipids, however, are potential acyl group donors through reaction with the ester functionality.…”

Section: Introductionmentioning

confidence: 99%

Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process

Dods

Bechinger

Mosely

et al. 2013

Journal of Molecular Biology

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. (2013) 'Acyl transfer from membrane lipids to peptides is a generic process.', Journal of molecular biology., 425 (22). pp. 4379-4387. Further information on publisher's website:http://dx.doi.org/10. 1016/j.jmb.2013.07.013 Publisher's copyright statement: NOTICE: this is the author's version of a work that was accepted for publication in Journal of molecular biology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reected in this document. Changes may have been made to this work since it was submitted for publication. A denitive version was subsequently published in Journal of molecular biology, 425, 22, 2013, 10.1016/j.jmb.2013.07.013 Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details. Abstract: The generality of acyl transfer from phospholipids to membrane-active peptides has been probed using liquid chromatography-mass spectrometry (LC-MS) analysis of peptide-lipid mixtures. The peptides examined include melittin, magainin II, PGLa, LAK1, LAK3 and penetratin. Peptides were added to liposomes with membrane lipid compositions ranging from pure phosphatidylcholine (PC) to mixtures of PC with phosphatidylethanolamine (PE), phosphatidylserine (PS) or phosphatidylglycerol (PG). Experiments were typically conducted at pH 7.4 at modest salt concentrations (90 mM NaCl). In favorable cases, lipidated peptides were further characterised by tandem MS methods to determine the sites of acylation. Melittin and magainin II were the most reactive peptides, with significant acyl transfer detected under all conditions and membrane compositions. Both peptides were lipidated at the N-terminus by transfer from PC, PE, PS or PG, as well as at internal sites: lysine for melittin; serine and lysine for magainin II. Acyl transfer could be detected within 3 hours of melittin addition to negatively charged membranes. The other peptides were less reactive, but for each peptide, acylation was found to occur in at least one of the conditions examined. The data demonstrate that acyl transfer is a generic process for peptides bound to membranes composed of diacylglycerophospholipids. Phospholipid membranes cannot therefore be considered as chemically inert towards peptides, and by extension proteins. *Graphical Abstract (for review)HIGHLIGHTS  The scope of acyl transfer from lipids to peptides has been probed  Melittin undergoes lipidation over a broad range of conditions  Magainin II is readily lipidated, bu...

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Resolving the kinetics of lipid, protein and peptide diffusion in membranes

Cited by 33 publications

References 211 publications

Mechanical coupling of microtubule-dependent motor teams during peroxisome transport in Drosophila S2 cells

Mechanical coupling of microtubule-dependent motor teams during peroxisome transport in Drosophila S2 cells

Dynamics of Lipids, Cholesterol, and Transmembrane α-Helices from Microsecond Molecular Dynamics Simulations

Acyl Transfer from Membrane Lipids to Peptides Is a Generic Process

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