TY - JOUR
T1 - Dynamic spatial and structural organization in artificial cells regulates signal processing by protein scaffolding
AU - Buddingh, Bastiaan C.
AU - Llopis-Lorente, Antoni
AU - Abdelmohsen, Loai K.E.A.
AU - van Hest, Jan C.M.
PY - 2020/12/21
Y1 - 2020/12/21
N2 - Structural and spatial organization are fundamental properties of biological systems that allow cells to regulate a wide range of biochemical processes. This organization is often transient and governed by external cues that initiate dynamic self-assembly processes. The construction of synthetic cell-like materials with similar properties requires the hierarchical and reversible organization of selected functional components on molecular scaffolds to dynamically regulate signaling pathways. The realization of such transient molecular programs in synthetic cells, however, remains underexplored due to the associated complexity of such hierarchical platforms. In this contribution, we effectuate dynamic spatial organization of effector protein subunits in a synthetic biomimetic compartment, a giant unilamellar vesicle (GUV), by associating in a reversible manner two fragments of a split luciferase to the membrane. This induces their structural dimerization, which consequently leads to the activation of enzymatic signaling. Importantly, such organization and activation are dynamic processes, and can be autonomously regulated-thus opening up avenues toward continuous spatiotemporal control over supramolecular organization and signaling in an artificial cell.
AB - Structural and spatial organization are fundamental properties of biological systems that allow cells to regulate a wide range of biochemical processes. This organization is often transient and governed by external cues that initiate dynamic self-assembly processes. The construction of synthetic cell-like materials with similar properties requires the hierarchical and reversible organization of selected functional components on molecular scaffolds to dynamically regulate signaling pathways. The realization of such transient molecular programs in synthetic cells, however, remains underexplored due to the associated complexity of such hierarchical platforms. In this contribution, we effectuate dynamic spatial organization of effector protein subunits in a synthetic biomimetic compartment, a giant unilamellar vesicle (GUV), by associating in a reversible manner two fragments of a split luciferase to the membrane. This induces their structural dimerization, which consequently leads to the activation of enzymatic signaling. Importantly, such organization and activation are dynamic processes, and can be autonomously regulated-thus opening up avenues toward continuous spatiotemporal control over supramolecular organization and signaling in an artificial cell.
UR - http://www.scopus.com/inward/record.url?scp=85098182387&partnerID=8YFLogxK
U2 - 10.1039/d0sc03933k
DO - 10.1039/d0sc03933k
M3 - Article
C2 - 34094478
AN - SCOPUS:85098182387
VL - 11
SP - 12829
EP - 12834
JO - Chemical Science
JF - Chemical Science
SN - 2041-6520
IS - 47
ER -