Membrane-sculpting BAR domains generate stable lipid microdomains

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Membrane-sculpting BAR domains generate stable lipid microdomains. / Zhao, Hongxia; Michelot, Alphée; Koskela, Essi V.; Tkach, Vadym; Stamou, Dimitrios; Drubin, David G.; Lappalainen, Pekka.

In: Cell Reports, Vol. 4, No. 6, 2013, p. 1213-1223.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Zhao, H, Michelot, A, Koskela, EV, Tkach, V, Stamou, D, Drubin, DG & Lappalainen, P 2013, 'Membrane-sculpting BAR domains generate stable lipid microdomains', Cell Reports, vol. 4, no. 6, pp. 1213-1223. https://doi.org/10.1016/j.celrep.2013.08.024

APA

Zhao, H., Michelot, A., Koskela, E. V., Tkach, V., Stamou, D., Drubin, D. G., & Lappalainen, P. (2013). Membrane-sculpting BAR domains generate stable lipid microdomains. Cell Reports, 4(6), 1213-1223. https://doi.org/10.1016/j.celrep.2013.08.024

Vancouver

Zhao H, Michelot A, Koskela EV, Tkach V, Stamou D, Drubin DG et al. Membrane-sculpting BAR domains generate stable lipid microdomains. Cell Reports. 2013;4(6):1213-1223. https://doi.org/10.1016/j.celrep.2013.08.024

Author

Zhao, Hongxia ; Michelot, Alphée ; Koskela, Essi V. ; Tkach, Vadym ; Stamou, Dimitrios ; Drubin, David G. ; Lappalainen, Pekka. / Membrane-sculpting BAR domains generate stable lipid microdomains. In: Cell Reports. 2013 ; Vol. 4, No. 6. pp. 1213-1223.

Bibtex

@article{94212004ebdf475d80508de5ab912401,

title = "Membrane-sculpting BAR domains generate stable lipid microdomains",

abstract = "Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of many cellular processes involving membrane dynamics. BAR domains sculpt phosphoinositide-rich membranes to generate membrane protrusions or invaginations. Here, we report that, in addition to regulating membrane geometry, BAR domains can generate extremely stable lipid microdomains by {"}freezing{"} phosphoinositide dynamics. This is a general feature of BAR domains, because the yeast endocytic BAR and Fes/CIP4 homology BAR (F-BAR) domains, the inverse BAR domain of Pinkbar, and the eisosomal BAR protein Lsp1 induced phosphoinositide clustering and halted lipid diffusion, despite differences in mechanisms of membrane interactions. Lsp1 displays comparable low diffusion rates in vitro and in vivo, suggesting that BAR domain proteins also generate stable phosphoinositide microdomains in cells. These results uncover a conserved role for BAR superfamily proteins in regulating lipid dynamics within membranes. Stable microdomains induced by BAR domain scaffolds and specific lipids can generate phase boundaries and diffusion barriers, which may have profound impacts on diverse cellular processes.",

author = "Hongxia Zhao and Alph{\'e}e Michelot and Koskela, {Essi V.} and Vadym Tkach and Dimitrios Stamou and Drubin, {David G.} and Pekka Lappalainen",

year = "2013",

doi = "10.1016/j.celrep.2013.08.024",

language = "English",

volume = "4",

pages = "1213--1223",

journal = "Cell Reports",

issn = "2211-1247",

publisher = "Cell Press",

number = "6",

}

RIS

TY - JOUR

T1 - Membrane-sculpting BAR domains generate stable lipid microdomains

AU - Zhao, Hongxia

AU - Michelot, Alphée

AU - Koskela, Essi V.

AU - Tkach, Vadym

AU - Stamou, Dimitrios

AU - Drubin, David G.

AU - Lappalainen, Pekka

PY - 2013

Y1 - 2013

N2 - Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of many cellular processes involving membrane dynamics. BAR domains sculpt phosphoinositide-rich membranes to generate membrane protrusions or invaginations. Here, we report that, in addition to regulating membrane geometry, BAR domains can generate extremely stable lipid microdomains by "freezing" phosphoinositide dynamics. This is a general feature of BAR domains, because the yeast endocytic BAR and Fes/CIP4 homology BAR (F-BAR) domains, the inverse BAR domain of Pinkbar, and the eisosomal BAR protein Lsp1 induced phosphoinositide clustering and halted lipid diffusion, despite differences in mechanisms of membrane interactions. Lsp1 displays comparable low diffusion rates in vitro and in vivo, suggesting that BAR domain proteins also generate stable phosphoinositide microdomains in cells. These results uncover a conserved role for BAR superfamily proteins in regulating lipid dynamics within membranes. Stable microdomains induced by BAR domain scaffolds and specific lipids can generate phase boundaries and diffusion barriers, which may have profound impacts on diverse cellular processes.

AB - Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of many cellular processes involving membrane dynamics. BAR domains sculpt phosphoinositide-rich membranes to generate membrane protrusions or invaginations. Here, we report that, in addition to regulating membrane geometry, BAR domains can generate extremely stable lipid microdomains by "freezing" phosphoinositide dynamics. This is a general feature of BAR domains, because the yeast endocytic BAR and Fes/CIP4 homology BAR (F-BAR) domains, the inverse BAR domain of Pinkbar, and the eisosomal BAR protein Lsp1 induced phosphoinositide clustering and halted lipid diffusion, despite differences in mechanisms of membrane interactions. Lsp1 displays comparable low diffusion rates in vitro and in vivo, suggesting that BAR domain proteins also generate stable phosphoinositide microdomains in cells. These results uncover a conserved role for BAR superfamily proteins in regulating lipid dynamics within membranes. Stable microdomains induced by BAR domain scaffolds and specific lipids can generate phase boundaries and diffusion barriers, which may have profound impacts on diverse cellular processes.

U2 - 10.1016/j.celrep.2013.08.024

DO - 10.1016/j.celrep.2013.08.024

M3 - Journal article

C2 - 24055060

VL - 4

SP - 1213

EP - 1223

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 6

ER -

ID: 92033352

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