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  Surface properties determining passage rates of proteins through nuclear pores.

Frey, S., Rees, R., Schünemann, J., Ng, S. C., Fünfgeld, K., Huyton, T., et al. (2018). Surface properties determining passage rates of proteins through nuclear pores. Cell, 174(1), 202-217. doi:10.1016/j.cell.2018.05.045.

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2609078_Suppl_1.pdf (Supplementary material), 205KB
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 Creators:
Frey, S.1, Author           
Rees, R.1, Author           
Schünemann, J.1, Author           
Ng, S. C.1, Author           
Fünfgeld, K.1, Author           
Huyton, T.1, Author           
Görlich, D.1, Author           
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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Free keywords: nuclear pore complex, permeability barrier, phase separation, hydrogel, cargo, importin, exportin, NTF2, protein homeostasis, aggregation
 Abstract: Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport through an FG domain-controlled barrier. We now explore how surface-features of a mobile species determine its NPC passage rate. Negative charges and lysines impede passage. Hydrophobic residues, certain polar residues (Cys, His), and, surprisingly, charged arginines have striking translocation-promoting effects. Favorable cation-π interactions between arginines and FG-phenylalanines may explain this apparent paradox. Application of these principles to redesign the surface of GFP resulted in variants that show a wide span of transit rates, ranging from 35-fold slower than wild-type to ∼500 times faster, with the latter outpacing even naturally occurring nuclear transport receptors (NTRs). The structure of a fast and particularly FG-specific GFPNTR variant illustrates how NTRs can expose multiple regions for binding hydrophobic FG motifs while evading non-specific aggregation. Finally, we document that even for NTR-mediated transport, the surface-properties of the "passively carried" cargo can strikingly affect the translocation rate.

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Language(s): eng - English
 Dates: 2018-06-282018-06-28
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.cell.2018.05.045
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Title: Cell
Source Genre: Journal
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Pages: - Volume / Issue: 174 (1) Sequence Number: - Start / End Page: 202 - 217 Identifier: -