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Reconstituting ring-rafts in bud-mimicking topography of model membranes

Journal Article · · Nature Communications
DOI:https://doi.org/10.1038/ncomms5507· OSTI ID:1623953
 [1];  [2];  [2];  [2];  [3];  [4];  [5];  [6];  [3];  [2];  [7];  [2]
  1. Seoul National Univ. (Korea, Republic of). School of Electrical Engineering; DOE/OSTI
  2. Seoul National Univ. (Korea, Republic of). School of Electrical Engineering
  3. Seoul National Univ. (Korea, Republic of). School of Mechanical and Aerospace Engineering. World Class Univ. (WCU) Program of Multiscale Mechanical Design
  4. Univ. of Minnesota, Minneapolis, MN (United States). Dept. of Biomedical Engineering
  5. Univ. of Minnesota, Minneapolis, MN (United States). Dept. of Biomedical Engineering and Chemical Engineering and Materials Science
  6. Univ. of Minnesota, Minneapolis, MN (United States). Dept. of Biomedical Engineering; Univ. of Minnesota, Minneapolis, MN (United States). Dept. of Biomedical Engineering and Chemical Engineering and Materials Science
  7. Univ. of California, Davis, CA (United States). Dept. of Biomedical Engineering and Chemical Engineering and Materials Science; Nanyang Technological Univ. (Singapore). School of Materials Science and Engineering. Centre for Biomimetic Sensor Science
During vesicular trafficking and release of enveloped viruses, the budding and fission processes dynamically remodel the donor cell membrane in a protein- or a lipid-mediated manner. In all cases, in addition to the generation or relief of the curvature stress, the buds recruit specific lipids and proteins from the donor membrane through restricted diffusion for the development of a ring-type raft domain of closed topology. Here, by reconstituting the bud topography in a model membrane, we demonstrate the preferential localization of cholesterol- and sphingomyelin-enriched microdomains in the collar band of the bud-neck interfaced with the donor membrane. The geometrical approach to the recapitulation of the dynamic membrane reorganization, resulting from the local radii of curvatures from nanometre-to-micrometre scales, offers important clues for understanding the active roles of the bud topography in the sorting and migration machinery of key signalling proteins involved in membrane budding.
Research Organization:
Univ. of California, Davis, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Materials Sciences & Engineering Division
Grant/Contract Number:
FG02-04ER46173
OSTI ID:
1623953
Journal Information:
Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 5; ISSN 2041-1723
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (9)

Minimally disruptive optical control of protein tyrosine phosphatase 1B journal February 2020
Continuity of Monolayer-Bilayer Junctions for Localization of Lipid Raft Microdomains in Model Membranes journal May 2016
Functional organization of the HIV lipid envelope journal September 2016
Carboxypeptidase O is a lipid droplet-associated enzyme able to cleave both acidic and polar C-terminal amino acids journal November 2018
Reversible Electrochemically Triggered Delamination Blistering of Hydrogel Films on Micropatterned Electrodes journal March 2016
To infect or not to infect: molecular determinants of bacterial outer membrane vesicle internalization by host membranes journal February 2020
Cholesterol Alters the Dynamics of Release in Protein Independent Cell Models for Exocytosis journal September 2016
Structured clustering of the glycosphingolipid GM1 is required for membrane curvature induced by cholera toxin journal June 2020
To infect or not to infect: molecular determinants of bacterial outer membrane vesicle internalization by host membranes posted_content September 2019

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