BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature

Kenneth Lindegaard Madsen; V K Bhatia; U Gether; D Stamou

doi:10.1016/j.febslet.2010.01.053

BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature

Kenneth Lindegaard Madsen, V K Bhatia, U Gether, D Stamou

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

81 Citationer (Scopus)

Abstract

Udgivelsesdato: 2010-May-3

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	584
Udgave nummer	9
Sider (fra-til)	1848-55
Antal sider	7
ISSN	0014-5793
DOI	https://doi.org/10.1016/j.febslet.2010.01.053
Status	Udgivet - 2010

Bibliografisk note

Adgang til dokumentet

10.1016/j.febslet.2010.01.053

Citationsformater

@article{8fc092d0b0f611df825b000ea68e967b,

title = "BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature",

abstract = "The internal membranes of eukaryotic cells are all twists and bends characterized by high curvature. During recent years it has become clear that specific proteins sustain these curvatures while others simply recognize membrane shape and use it as {"}molecular information{"} to organize cellular processes in space and time. Here we discuss this new important recognition process termed membrane curvature sensing (MCS). First, we review a new fluorescence-based experimental method that allows characterization of MCS using measurements on single vesicles and compare it to sensing assays that use bulk/ensemble liposome samples of different mean diameter. Next, we describe two different MCS protein motifs (amphipathic helices and BAR domains) and suggest that in both cases curvature sensitive membrane binding results from asymmetric insertion of hydrophobic amino acids in the lipid membrane. This mechanism can be extended to include the insertion of alkyl chain in the lipid membrane and consequently palmitoylated and myristoylated proteins are predicted to display similar curvature sensitive binding. Surprisingly, in all the aforementioned cases, MCS is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity as assumed so far. Finally, we integrate these new insights into the debate about which motifs are involved in sensing versus induction of membrane curvature and what role MCS proteins may play in biology.",

author = "Madsen, {Kenneth Lindegaard} and Bhatia, {V K} and U Gether and D Stamou",

note = "Keywords: Animals; Biosensing Techniques; Fluorescence; Glycosylphosphatidylinositols; Humans; Hydrophobicity; Membrane Fluidity; Membrane Proteins; Models, Biological; Models, Molecular; Protein Binding; Protein Structure, Secondary",

year = "2010",

doi = "10.1016/j.febslet.2010.01.053",

language = "English",

volume = "584",

pages = "1848--55",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "9",

}

TY - JOUR

T1 - BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature

AU - Madsen, Kenneth Lindegaard

AU - Bhatia, V K

AU - Gether, U

AU - Stamou, D

N1 - Keywords: Animals; Biosensing Techniques; Fluorescence; Glycosylphosphatidylinositols; Humans; Hydrophobicity; Membrane Fluidity; Membrane Proteins; Models, Biological; Models, Molecular; Protein Binding; Protein Structure, Secondary

PY - 2010

Y1 - 2010

N2 - The internal membranes of eukaryotic cells are all twists and bends characterized by high curvature. During recent years it has become clear that specific proteins sustain these curvatures while others simply recognize membrane shape and use it as "molecular information" to organize cellular processes in space and time. Here we discuss this new important recognition process termed membrane curvature sensing (MCS). First, we review a new fluorescence-based experimental method that allows characterization of MCS using measurements on single vesicles and compare it to sensing assays that use bulk/ensemble liposome samples of different mean diameter. Next, we describe two different MCS protein motifs (amphipathic helices and BAR domains) and suggest that in both cases curvature sensitive membrane binding results from asymmetric insertion of hydrophobic amino acids in the lipid membrane. This mechanism can be extended to include the insertion of alkyl chain in the lipid membrane and consequently palmitoylated and myristoylated proteins are predicted to display similar curvature sensitive binding. Surprisingly, in all the aforementioned cases, MCS is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity as assumed so far. Finally, we integrate these new insights into the debate about which motifs are involved in sensing versus induction of membrane curvature and what role MCS proteins may play in biology.

AB - The internal membranes of eukaryotic cells are all twists and bends characterized by high curvature. During recent years it has become clear that specific proteins sustain these curvatures while others simply recognize membrane shape and use it as "molecular information" to organize cellular processes in space and time. Here we discuss this new important recognition process termed membrane curvature sensing (MCS). First, we review a new fluorescence-based experimental method that allows characterization of MCS using measurements on single vesicles and compare it to sensing assays that use bulk/ensemble liposome samples of different mean diameter. Next, we describe two different MCS protein motifs (amphipathic helices and BAR domains) and suggest that in both cases curvature sensitive membrane binding results from asymmetric insertion of hydrophobic amino acids in the lipid membrane. This mechanism can be extended to include the insertion of alkyl chain in the lipid membrane and consequently palmitoylated and myristoylated proteins are predicted to display similar curvature sensitive binding. Surprisingly, in all the aforementioned cases, MCS is predominantly mediated by a higher density of binding sites on curved membranes instead of higher affinity as assumed so far. Finally, we integrate these new insights into the debate about which motifs are involved in sensing versus induction of membrane curvature and what role MCS proteins may play in biology.

U2 - 10.1016/j.febslet.2010.01.053

DO - 10.1016/j.febslet.2010.01.053

M3 - Journal article

C2 - 20122931

SN - 0014-5793

VL - 584

SP - 1848

EP - 1855

JO - FEBS Letters

JF - FEBS Letters

IS - 9

ER -