PUBLICATION

Tunable assembly of protein-microdomains in living vertebrate embryos

Authors
Li, Z., Tyrpak, D.R., MacKay, J.A., Lien, C.L.
ID
ZDB-PUB-191218-1
Date
2018
Source
Advanced biosystems   2(10): (Journal)
Registered Authors
Lien, Ching-Ling (Ellen)
Keywords
elastin-like polypeptides, genetically engineered protein microdomains, protein assembly, thermo-responsive protein polymers, zebrafish
MeSH Terms
none
PubMed
31840042 Full text @ Adv Biosyst
Abstract
Subcellular events such as trafficking and signaling are regulated by self-assembled protein complexes inside the cell. The ability to rapidly and reversibly manipulate these protein complexes would likely enhance studies of their mechanisms and their roles in biological function and disease manifestation.[1, 2] This manuscript reports that thermally-responsive elastin-like polypeptides (ELPs) linked to fluorescent proteins can regulate the self-assembly and disassembly of protein microdomains within the individual cells of zebrafish embryos. By exploring a library of fluorescent ELP proteins, this reports demonstrates that ELPs can co-assemble different fluorescent proteins inside of embryos. By tuning ELP length and sequence, fluorescent protein microdomains can be assembled at different temperatures, in varying sizes, or for desired periods of time. For the first time in a multicellular living embryo, these studies demonstrate that temperature-mediated ELP assembly can reversibly manipulate assembly of subcellular protein complexes, which may have applications in the study and manipulation of in vivo biological functions.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping