Membrane fusion articles within Nature

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• Letter | 01 November 2017

  A tethering complex drives the terminal stage of SNARE-dependent membrane fusion

  Tethering proteins, known to mediate initial recognition and attachment during membrane fusion, are essential for driving the transition from the hemifused state to fusion pore formation.

  • Massimo D’Agostino
  • , Herre Jelger Risselada
  •  & Andreas Mayer

• Letter | 24 August 2016

  An endosomal tether undergoes an entropic collapse to bring vesicles together

  A new endosomal tethering mechanism involving a mechanochemical cycle of the dimeric coiled-coil protein EEA1 regulated by Rab5:GTP binding and GTP hydrolysis.

  • David H. Murray
  • , Marcus Jahnel
  •  & Marino Zerial

• Letter | 29 June 2015

  A hemi-fission intermediate links two mechanistically distinct stages of membrane fission

  The GTPase dynamin provides the driving force for fission of membrane-bound vesicular structures; here, it is shown that dynamin-driven membrane fission proceeds in two mechanistically distinct stages that are separated by a metastable hemi-fission intermediate that requires GTP hydrolysis for progression to full fission.

  • Juha-Pekka Mattila
  • , Anna V. Shnyrova
  •  & Vadim A. Frolov

• Letter | 03 June 2015

  ESCRT-III controls nuclear envelope reformation

  The ESCRT-III complex is implicated in the reformation of the nuclear envelope; the CHMP2A component of ESCRT-III is directed to the forming nuclear envelope through classical ESCRT-assembly mechanisms, with the help of the p97 complex component UFD1, and provides an activity essential for nuclear envelope reformation.

  • Yolanda Olmos
  • , Lorna Hodgson
  •  & Jeremy G. Carlton