Cell Biochemistry and Biophysics

, Volume 50, Issue 2, pp 79–109 | Cite as

Composition-driven Surface Domain Structuring Mediated by Sphingolipids and Membrane-active Proteins

Above the Nano- but under the Micro-scale: Mesoscopic Biochemical/Structural Cross-talk in Biomembranes
  • Bruno Maggio
  • Graciela A. Borioli
  • Maximiliano Del Boca
  • Luisina De Tullio
  • María L. Fanani
  • Rafael G. Oliveira
  • Carla M. Rosetti
  • Natalia Wilke
Review Paper


Biomembranes contain a wide variety of lipids and proteins within an essentially two-dimensional structure. The coexistence of such a large number of molecular species causes local tensions that frequently relax into a phase or compositional immiscibility along the lateral and transverse planes of the interface. As a consequence, a substantial microheterogeneity of the surface topography develops and that depends not only on the lipid–protein composition, but also on the lateral and transverse tensions generated as a consequence of molecular interactions. The presence of proteins, and immiscibility among lipids, constitute major perturbing factors for the membrane sculpturing both in terms of its surface topography and dynamics. In this work, we will summarize some recent evidences for the involvement of membrane-associated, both extrinsic and amphitropic, proteins as well as membrane-active phosphohydrolytic enzymes and sphingolipids in driving lateral segregation of phase domains thus determining long-range surface topography.


Gangliosides Glycosphingolipid-enriched domains Membrane topology Epifluorescence microscopy Brewster angle microscopy Phospholipases Sphingomyelinase Transcription factors c-Fos c-Jun Myelin Electrostatic field Phase-segregated domains 





N-acylsphingosine (ceramide)







Gg4Cer (asialo-GM1)


GM1 (II3NeuAc-CgOse4Cer)



















Phosphatidylinositol bisphosphate








1,2-Dipalmitoyl-sn-phosphoethanolamine-N-[lyssamine rhodamine B sulfonyl]


1,1′-Didodecyl-3,3,3′,3′-tetramethylindocarbocyanine perchlorate


Hexagonal I (micellar) phase


Hexagonal II (inverse micellar) phase


Phospholipase A2


Phospholipase C




Myelin basic protein


Folch’s proteolipid


Myristoylated alanine-rich C-kinase substrate


Transition temperature


Infrared spectroscopy


Electron paramagnetic resonance


Brewster angle microscopy.



This work was supported by: SECyT-UNC, CONICET and FONCyT (Argentina); B.M., G.A.B, M.L.F., R.G.O. and N.W. are Career Investigators of CONICET; M.D.B. and C.M.R. are Doctoral Fellows of CONICET; and L.D. is a Doctoral Fellow of FONCYT. R. G. O. thanks The Alexander von Humboldt Foundation for a Research Fellowship.


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Copyright information

© Humana Press Inc. 2007

Authors and Affiliations

  • Bruno Maggio
    • 1
  • Graciela A. Borioli
    • 1
  • Maximiliano Del Boca
    • 1
  • Luisina De Tullio
    • 1
  • María L. Fanani
    • 1
  • Rafael G. Oliveira
    • 1
  • Carla M. Rosetti
    • 1
  • Natalia Wilke
    • 1
  1. 1.Departamento de Química Biológica, Facultad de Ciencias Químicas, Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC)Universidad Nacional de Córdoba – CONICETCordobaArgentina

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