Literature DB >> 21320438

Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C.

Sergio Alonso1, Undine Dietrich, Chris Händel, Josef A Käs, Markus Bär.   

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.
Copyright © 2011 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 21320438      PMCID: PMC3037601          DOI: 10.1016/j.bpj.2010.12.3702

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  23 in total

1.  Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane.

Authors:  M Thelen; A Rosen; A C Nairn; A Aderem
Journal:  Nature       Date:  1991-05-23       Impact factor: 49.962

2.  Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin.

Authors:  A Arbuzova; J Wang; D Murray; J Jacob; D S Cafiso; S McLaughlin
Journal:  J Biol Chem       Date:  1997-10-24       Impact factor: 5.157

3.  Travelling lipid domains in a dynamic model for protein-induced pattern formation in biomembranes.

Authors:  Karin John; Markus Bär
Journal:  Phys Biol       Date:  2005-06       Impact factor: 2.583

4.  A pleckstrin homology domain specific for phosphatidylinositol 4, 5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis.

Authors:  R W Holz; M D Hlubek; S D Sorensen; S K Fisher; T Balla; S Ozaki; G D Prestwich; E L Stuenkel; M A Bittner
Journal:  J Biol Chem       Date:  2000-06-09       Impact factor: 5.157

5.  A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha.

Authors:  Senena Corbalán-García; Josefa García-García; José A Rodríguez-Alfaro; Juan C Gómez-Fernández
Journal:  J Biol Chem       Date:  2002-11-07       Impact factor: 5.157

6.  MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin.

Authors:  J H Hartwig; M Thelen; A Rosen; P A Janmey; A C Nairn; A Aderem
Journal:  Nature       Date:  1992-04-16       Impact factor: 49.962

Review 7.  Plasma membrane phosphoinositide organization by protein electrostatics.

Authors:  Stuart McLaughlin; Diana Murray
Journal:  Nature       Date:  2005-12-01       Impact factor: 49.962

8.  Supplementation of the phosphatidyl-L-serine requirement of protein kinase C with nonactivating phospholipids.

Authors:  M H Lee; R M Bell
Journal:  Biochemistry       Date:  1992-06-09       Impact factor: 3.162

Review 9.  Lipid domain formation and dynamics in giant unilamellar vesicles explored by fluorescence correlation spectroscopy.

Authors:  Nicoletta Kahya; Dag Scherfeld; Kirsten Bacia; Petra Schwille
Journal:  J Struct Biol       Date:  2004-07       Impact factor: 2.867

10.  A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C.

Authors:  Jonathan D Violin; Jin Zhang; Roger Y Tsien; Alexandra C Newton
Journal:  J Cell Biol       Date:  2003-06-02       Impact factor: 10.539

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