English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Interaction of membrane-spanning proteins with peripheral and lipid-anchored membrane proteins: perspectives from protein- lipid interactions (Review)

MPS-Authors
/persons/resource/persons15495

Marsh,  D.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15247

Horvath,  L. I.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15900

Swamy,  M. J.
Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)

17152.pdf
(Publisher version), 0B

Supplementary Material (public)
There is no public supplementary material available
Citation

Marsh, D., Horvath, L. I., Swamy, M. J., Mantripragada, S., & Kleinschmidt, J. H. (2002). Interaction of membrane-spanning proteins with peripheral and lipid-anchored membrane proteins: perspectives from protein- lipid interactions (Review). Molecular Membrane Biology, 19(4), 247-255. Retrieved from http://informahealthcare.com/doi/pdf/10.1080/09687680210162419.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F2E4-7
Abstract
Studies of lipid-protein interactions in double-reconstituted systems involving both integral and peripheral or lipid- anchored proteins are reviewed. Membranes of climyristoyl phosphatidylglycerol containing either myelin proteolipid protein or cytochrome c oxidase were studied. The partner peripheral proteins bound to these membranes were myelin basic protein or cytochrome c, respectively. In addition, the interactions between the myelin proteolipid protein and avidin that was membrane-anchored by binding to N-biotinyl phosphatidylethanolamine were studied in dimyristoyl phosphatidylcholine membranes. Steric exclusion plays a significant role when sizes of the peripheral protein and transmembrane domain of the integral protein are comparable. Even so, the effects on avidin-linked lipids are different from those induced by myelin basic protein on freely diffusible lipids, both interacting with the myelin proteolipid protein. Both the former and the cytochrome c/cytochrome oxidase couple evidence a propagation of lipid perturbation out from the intramembrane protein interface that could be a basis for formation of microdomains.