Dependence of M13 Major Coat Protein Oligomerization and Lateral Segregation on Bilayer Composition

Fernandes, Fábio; Loura, Luís M. S.; Prieto, Manuel; Koehorst, R.B.M.; Spruijt, Ruud B.; Hemminga, M.A.

doi:10.1016/s0006-3495(03)74666-9

Cited by 40 publications

(41 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Parameters that determine these energy costs include the extent of mismatch between the protein and the lipids, the length difference between the lipids, the mixing behavior of the pure lipids, and specific properties of the proteins or peptides. The lipid compositions investigated in the present study closely resemble those previously used in fluorescence studies, in which some preferential interactions were in fact observed (5,7,8,31). However, the properties of the peptides and proteins used in the various studies are very different, and it is important to note that even small changes in amino acid sequence of a transmembrane peptide can result in very different behavior of a peptide/lipid system.…”

Section: Discussionsupporting

confidence: 75%

“…This conclusion is further substantiated by the results of the mixtures of the unsaturated PC species. Also in these systems no molecular sorting takes place under Literature data so far have shown molecular sorting of lipids to occur to various extents for a number of membrane proteins (5)(6)(7)(8). Then why do we not observe it in our systems?…”

Section: Discussionmentioning

confidence: 69%

“…Previously, this has been probed mainly by fluorescence and ESR 1 methods using labeled lipids (5)(6)(7)(8)(9)(10)(11). In this study, we explore a more direct method to investigate the immediate surroundings of membrane proteins.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Photo-Crosslinking Analysis of Preferential Interactions between a Transmembrane Peptide and Matching Lipids

et al. 2004

View full text Add to dashboard Cite

In this study, a novel method is presented by which the molecular environment of a transmembrane peptide can be investigated directly. This was achieved by incorporating a photoactivatable crosslinking probe in the hydrophobic segment of a model transmembrane peptide. When this peptide was incorporated into lipid bilayers and irradiated with UV light, a covalent bond was formed between the crosslinking probe and a lipid. This crosslinking reaction could be visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the resulting product could be characterized by mass spectrometry. By use of phospholipases, it was demonstrated that the peptide crosslinks to both acyl chains of the lipids. The peptide showed a clear preference to partition into fluid lipids and was excluded from lipids in the gel phase. However, when the peptide was incorporated into bilayers containing two lipid species with different acyl chain lengths, molecular sorting of the lipids around the peptide based on hydrophobic matching was not observed. It is proposed that the size of the transmembrane part plays an important role in the dynamic interactions of membrane proteins with the surrounding lipids and hence in determining whether molecular sorting can occur.Proteins in biological membranes reside in a complex environment in which they are surrounded by many different lipid species. Transmembrane proteins can have different affinities for different lipids, and as a result particular lipids or members of particular lipid classes may become enriched around a certain protein. Such differences in affinity may be due to specific interactions with the lipid headgroups or the lipid acyl chains. An example of the latter would be the enrichment of matching lipids around a protein, which could be a mechanism by which mismatches between hydrophobic transmembrane segments and the hydrophobic thickness of the lipid bilayer can be relieved. Such a mechanism of molecular sorting by transmembrane proteins has been predicted from theoretical calculations (1, 2; reviewed in refs 3 and 4) and has indeed been shown to occur for several transmembrane proteins (5-8).To gain insight into the role of protein-lipid interactions in the sorting of lipids around specific proteins, tools must be available to determine the lipid environment of membrane proteins. Previously, this has been probed mainly by fluorescence and ESR 1 methods using labeled lipids (5-11). In this study, we explore a more direct method to investigate the immediate surroundings of membrane proteins. For this purpose we make use of a synthetic model peptide, which contains a photoactivatable probe that is able to form covalent bonds with the surrounding lipids upon UV irradiation. The crosslinking reaction can be visualized by SDS-PAGE analysis and the identity of the lipid that is crosslinked to the peptide can subsequently be characterized by mass spectrometry.

show abstract

Section: Discussionsupporting

confidence: 75%

Section: Discussionmentioning

confidence: 69%

See 1 more Smart Citation

Photo-Crosslinking Analysis of Preferential Interactions between a Transmembrane Peptide and Matching Lipids

et al. 2004

View full text Add to dashboard Cite

show abstract

“…A possible explanation for the function of MAL is that both lateral segregation of lipids and protein aggregation (OC formation) are facilitated at least in part by positive hydrophobic mismatching between the length of the MAL's TMDs and the average width of the hydrophobic fatty acyl core of the membrane (Fernandes et al, 2003;Jensen and Mouritsen, 2004;Engelman, 2005;Hancock, 2006). To further pursue this hypothesis, we applied site-directed mutagenesis to the DiHcRED-MAL chimera.…”

Section: Mutagenesis Of Dihcred-mal and Bifc Analysismentioning

confidence: 99%

“…Hence, membrane lipids may yield by bending as well as by selective accumulation of lipids with matching tail lengths (Kuzmin et al, 2005). Alternatively, positively mismatched membrane proteins have been shown to respond to mismatch with the surrounding lipids by aggregating, to minimize the mismatched contact zones (Gil et al, 1997;Fernandes et al, 2003), although substantial aggregation requires additional binding inducement in the form of protein-protein interactions (Sperotto and Mouritsen, 1991). In general, liquid ordered domains are thicker than the surrounding liquiddisordered membrane.…”

Section: Introductionmentioning

confidence: 99%

Clustering and Lateral Concentration of Raft Lipids by the MAL Protein

Magal

Yaffe

Shepshelovich

et al. 2009

MBoC

View full text Add to dashboard Cite

MAL, a compact hydrophobic, four-transmembrane-domain apical protein that copurifies with detergent-resistant membranes is obligatory for the machinery that sorts glycophosphatidylinositol (GPI)-anchored proteins and others to the apical membrane in epithelia. The mechanism of MAL function in lipid-raft-mediated apical sorting is unknown. We report that MAL clusters formed by two independent procedures-spontaneous clustering of MAL tagged with the tandem dimer DiHcRED (DiHcRED-MAL) in the plasma membrane of COS7 cells and antibody-mediated cross-linking of FLAG-tagged MAL-laterally concentrate markers of sphingolipid rafts and exclude a fluorescent analogue of phosphatidylethanolamine. Site-directed mutagenesis and bimolecular fluorescence complementation analysis demonstrate that MAL forms oligomers via xx intramembrane protein-protein binding motifs. Furthermore, results from membrane modulation by using exogenously added cholesterol or ceramides support the hypothesis that MAL-mediated association with raft lipids is driven at least in part by positive hydrophobic mismatch between the lengths of the transmembrane helices of MAL and membrane lipids. These data place MAL as a key component in the organization of membrane domains that could potentially serve as membrane sorting platforms.

show abstract

Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels

et al. 2015

View full text Add to dashboard Cite

Oriented circular dichroism was used to study the alignment crown ether-modified peptides. The influence of different N-and C-functionalities was assessed using at variable peptide:lipid ratios from 1:20 to 1:200. Neither the functionalities nor the concentration had any major effect on the orientation. The alignment of the 21-mer peptides was also examined with lipid membranes of different bilayer thickness. The use of synchrotron radiation as light source allowed the study of peptide:lipid molar ratios from 1:20 to 1:1000. For all conditions studied, the peptides were found to be predominantly incorporated as a transmembrane helix into the membrane, especially at low peptide concentration, but started to aggregate on the membrane surface at higher peptide:lipid ratios. The structural information on the preferred trans-bilayer alignment of the crown ether functional groups explains their ion conductivity and is useful for the further development of membrane-active nanochemotherapeutics.

show abstract

Dependence of M13 Major Coat Protein Oligomerization and Lateral Segregation on Bilayer Composition

Cited by 40 publications

References 55 publications

Photo-Crosslinking Analysis of Preferential Interactions between a Transmembrane Peptide and Matching Lipids

Photo-Crosslinking Analysis of Preferential Interactions between a Transmembrane Peptide and Matching Lipids

Clustering and Lateral Concentration of Raft Lipids by the MAL Protein

Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels

Contact Info

Product

Resources

About