Porins are bacterial β-strand proteins that form a water-filled β-barrel pore within the outer membrane, either causing a disruption of the membrane or generating a means for transporting molecules such as carbohydrates and amino acids across the membrane. Porins allow for passive diffusion and so are considered membrane transport proteins and channels.

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News and Comment

  • News & Views |

    Designing membrane proteins that function as ion channels is challenging. Now, peptides that self-assemble into water-soluble α-helical barrels have been repurposed to form ion channels in membranes by lining the interior with polar residues and the exterior with hydrophobic ones.

    • Giovanna Ghirlanda
    Nature Chemistry 13, 621-623
  • News & Views |

    Cryo-EM, crystallography, biochemical experiments and computational approaches have been used to study different intermediate states of the Aeromonas hydrophila toxin aerolysin en route to pore formation. These results reveal that an unexpected and marked rotation of the core aerolysin machinery is required to unleash the membrane-spanning regions.

    • James C Whisstock
    •  & Michelle A Dunstone
  • Research Highlights |

    Emerging evidence suggests an involvement of nuclear pore components in the regulation of neural differentiation and aging. These findings will have far-ranging impacts on the understanding of the function of the nuclear envelope in physiological settings and in various neurological diseases.

    • Guang-Hui Liu
    • , Mo Li
    •  & Juan Carlos Izpisua Belmonte
    Cell Research 22, 1212-1214