title: Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C.
abstract: The binding of the MARCKS peptide to the lipid monolayer containing PIP(2) increases the lateral pressure of the monolayer. The unbinding dynamics modulated by protein kinase C leads to oscillations in lateral pressure of lipid monolayers. These periodic dynamics can be attributed to changes in the crystalline lipid domain size. We have developed a mathematical model to explain these observations based on the changes in the physical structure of the monolayer by the translocation of MARCKS peptide. The model indicates that changes in lipid domain size drives these oscillations. The model is extended to an open system that sustains chemical oscillations.
authors.affiliation: Physikalisch-Technische Bundesanstalt, Berlin, Germany. sergio.alonso@ptb.de
authors.forename: Sergio
authors.initials: S
authors.lastname: Alonso
authors.forename: Undine
authors.initials: U
authors.lastname: Dietrich
authors.forename: Chris
authors.initials: C
authors.lastname: Händel
authors.forename: Josef A
authors.initials: JA
authors.lastname: Käs
authors.forename: Markus
authors.initials: M
authors.lastname: Bär
mesh_terms: D001692:Biological Transport; D003198:Computer Simulation; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism*; D008055:Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D017711:Nonlinear Dynamics; D010766:Phosphorylation; D011312:Pressure; D011493:Protein Kinase C / Q000378:metabolism*; D015290:Second Messenger Systems; D013997:Time Factors
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D008055:Lipids; D008565:Membrane Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011493:Protein Kinase C