Liposomes, Exosomes, and Virosomes: From Modeling Complex
Membrane Processes to Medical Diagnostics and Drug Delivery
Poster Abstracts
68
49-POS
Board 25
Membrane Nucleoporins Form Porous Proteoliposomes with Nuclear Pore-Like Selectivity
Radhakrishnan Panatala
1,2
, Suncica Vujica
1,2
, Yusuke Sakiyama
1,2
, Roderick Lim
1,2
,
2
Swiss Nanoscience Institute, Basel, Basel-Stadt, Switzerland.
1
Biozentrum, Basel, Basel-Stadt,
Switzerland,
Eukaryotic cells maintain order and function by the selective accumulation of essential
macromolecules in the nucleus. This process is regulated by soluble nuclear transport receptors
(NTRs) that gain exclusive access through 50 nm channels known as nuclear pore complexes
(NPCs). Here, we have engineered nanoporous proteoliposomes that harbor key membrane
proteins of the NPC. Using fluorescence-based translocation assays, we observed that these
proteoliposomes show to discriminate against non-specific macromolecules above a certain size-
threshold whereas specific transport factors are transported across the pores. Imported NTRs are
subsequently entrapped within the proteoliposome lumen using wheat germ agglutinin (WGA), a
known NPC blocking agent. In conjunction, we performed morphological characterization of the
nanopores by high-speed atomic force microscopy (HS-AFM), which revealed that the
permeability barrier, composed of FG-nucleoporins, resembles to that of NPCs from
X. laevis
oocyte nuclei. Eventually, we’d like to apply such a macromolecular logistics system to sort and
encapsulate specific molecular modules from a complex environment leading to the construction
of a molecular factory.