c-Jun interacts with phospholipids and c-Fos at the interface

Boca, Maximiliano Del; Caputto, Beatriz L.; Maggio, Bruno; Borioli, Graciela A.

doi:10.1016/j.jcis.2005.01.069

Cited by 10 publications

(12 citation statements)

References 38 publications

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“…Its critical concentration C *, based on surface potential dependence on subphase concentration C 0 , is 150 n M (Figure 1, inset). The C * of Fra‐1 is twice that of c‐Jun (75 n M )2 and three times that of c‐Fos (50 n M ) 28. Although small, such differences are observed in spite of the high homology of sequence between these proteins (44% homology between Fra‐1 and c‐Fos) and underline the complex nature of protein adsorption dependence on bulk concentration 41.…”

Section: Resultsmentioning

confidence: 94%

“…All curves are the average of at least duplicates with error ±0.3 m N m −1 and ±5 Å 2 . The measurements for curves for c‐Fos and c‐Jun are repetitions of those published in previous work2, 28 and were performed to compare with Fra‐1.…”

Section: Resultsmentioning

confidence: 99%

“…Surface dipole potential (Δ V ) was measured by a high impedance millivoltmeter connected to a surface ionizing 241 Å electrode positioned 5‐mm above the monolayer surface, and to a reference Ag/AgCl electrode connected to the aqueous subphase through a saline bridge. Absence of surface‐active impurities in the subphase and in the spreading solvents was routinely controlled 2. Isotherms were compressed at a constant rate of 640 Å 2 molecule −1 min −1 allowing for reproducibility.…”

Section: Methodsmentioning

confidence: 99%

“…Our studies on the amphitropic nature of c‐Fos and c‐Jun1, 2 ensued after the discovery that c‐Fos has a nontranscriptional role as modulator of phospholipid metabolism in association with endoplasmic reticulum 3. The surface properties of these proteins are relevant because their association to membranes may counterbalance dimerization in an instance of AP‐1 function regulation, and because they may affect membrane state and processes.…”

Section: Introductionmentioning

confidence: 99%

“…The surface properties of these proteins are relevant because their association to membranes may counterbalance dimerization in an instance of AP‐1 function regulation, and because they may affect membrane state and processes. The complex thermodynamics and kinetics of association of c‐Fos and c‐Jun, between them and with phospholipids on one hand,1, 2, 4 and the modulation of phospholipase activity through changes in substrate packing induced by c‐Fos on the other hand5, 6 appropriately illustrate both alternatives.…”

Section: Introductionmentioning

confidence: 99%

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The immediate‐early oncoproteins Fra‐1, c‐Fos, and c‐Jun have distinguishable surface behavior and interactions with phospholipids

et al. 2009

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This work explores the surface properties of the transcription factor Fra-1 and compares them with those of two other immediate early proteins, c-Fos and c-Jun, to establish generalities and differences in the surface behavior and interaction with phospholipids of this type of proteins. We present several experimental clues of the flexible nature of Fra-1, c-Fos, and c-Jun that support sequence-based predictions of their intrinsical disorder. The values of surface parameters for Fra-1 are similar in general to those of c-Fos and c-Jun. However, we find differences in the interactions of the three proteins with phospholipids. The closely related Fra-1 and c-Fos share affinity for anionic lipids but the former has more affinity for a condensed phase and senses a change in DPPC phase, while the latter has more affinity for an expanded phase. These features are in contrast with our previous finding that c-Jun is not selective for phospholipid polar head group or charge. We show here that at least some immediate early transcription factors can interact with membrane phospholipids in a distinguishable manner, and this shall provide a basis for their potential capacity to regulate membrane-mediated cellular processes.

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Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The immediate‐early oncoproteins Fra‐1, c‐Fos, and c‐Jun have distinguishable surface behavior and interactions with phospholipids

et al. 2009

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

Maggio

Borioli

Boca

et al. 2007

Cell Biochem Biophys

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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.

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