c-Fos is surface active and interacts differentially with phospholipid monolayers.
The transcription factor c-Fos forms stable Gibbs and Langmuir monolayers at the air-buffer interface. Its marked surface activity is enhanced by penetration into phospholipid films above the protein's own maximum adsorption surface pressure to a lipid-free interface. The protein-phospholipid stabilizing interactions at the interface depend on the lipid polar head group and the increases of lateral surface pressure generated are comparable to those of membrane-active proteins. The surface activity of c-Fos is strong enough to thermodynamically drive and retain c-Fos at the membrane interface where it may exert direct or indirect effects.
Borioli
G A
GA
Dpto. Química Biológica, CIQUIBIC, Facultad de Ciencias Químicas, Ciudad Universitaria, Pabellón Argentina, 5000 Córdoba, Argentina.
Caputto
B L
BL
Maggio
B
B
D016475:3T3 Cells; D000327:Adsorption; D000818:Animals; D003001:Cloning, Molecular; D004926:Escherichia coli; D007700:Kinetics; D008081:Liposomes / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D051379:Mice; D010743:Phospholipids / Q000737:chemistry*; D011312:Pressure; D016760:Proto-Oncogene Proteins c-fos / Q000737:chemistry* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013499:Surface Properties
D008081:Liposomes; D008563:Membrane Lipids; D010743:Phospholipids; D016760:Proto-Oncogene Proteins c-fos; D011994:Recombinant Proteins