FG repeats facilitate integral protein trafficking to the inner nuclear membrane

A.R.W. Kerr, E.C. Schirmer

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The mechanism for nucleo-cytoplasmic transport of integral membrane proteins is poorly understood compared to transport of soluble molecules. We recently demonstrated that at least four distinct mechanisms can contribute to transport of integral proteins through the peripheral channels of the nuclear pore complex. One of these requires having multiple phenylalanine-glycine (FG) pairings on the integral protein. It also requires the nuclear pore complex protein Nup35, which separately contains FG repeats. FG-repeats on nuclear pore complex proteins in the central channel have been proposed to interact with FGs on transport receptors to facilitate transport of soluble proteins. Here we show that FG repeats occur quite frequently in both transmembrane and soluble proteins identified in multiple separate proteomic analyses of nuclear envelopes. We postulate that the FG repeats enable these proteins to function as their own transport receptors.
Original languageEnglish
Pages (from-to)557-559
Number of pages3
JournalCommunicative and Integrative Biology
Issue number5
Publication statusPublished - 2011

Keywords / Materials (for Non-textual outputs)

  • nuclear envelope
  • inner nuclear membrane
  • outer nuclear membrane
  • endoplasmic reticulum
  • translocation
  • nucleoporin
  • phenylalanine-glycine repeats
  • nuclear pore complex
  • Nup35


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