Premium
Synthetic Biology: Flipping the Switch on Clathrin‐Mediated Endocytosis using Thermally Responsive Protein Microdomains (Adv. Funct. Mater. 34/2014)
Author(s) -
Pastuszka Martha K.,
Okamoto Curtis T.,
HammAlvarez Sarah F.,
MacKay J. Andrew
Publication year - 2014
Publication title -
advanced functional materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.069
H-Index - 322
eISSN - 1616-3028
pISSN - 1616-301X
DOI - 10.1002/adfm.201470224
Subject(s) - endocytosis , clathrin , internalization , receptor mediated endocytosis , microbiology and biotechnology , fusion protein , lipid microdomain , organelle , materials science , fusion , biophysics , receptor , biology , nanotechnology , biochemistry , membrane , recombinant dna , linguistics , philosophy , gene
Elastin‐like polypeptides can be expressed in eukaryotic cells in fusion with functional proteins. When heated, they assemble organelle‐sized microdomains that sequester target complexes. On page 5340, J. A. MacKay and team demonstrate that, by fusion to clathrin‐light chain, these microdomains co‐localize and sequester clathrin heavy chain, which is necessary for clathrin‐mediated endocytosis. Assembly rapidly and reversibly blocks internalization of G‐protein coupled receptors. Image created by Isaac Mora.