Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity

Journal Article

Like animals and plants, multicellular fungi possess cell-to-cell channels (septal pores) that allow intercellular communication and transport. Here, using a combination of MS of Woronin body-associated proteins and a bioinformatics approach that identifies related proteins based on composition and character, we identify 17 septal pore-associated (SPA) proteins that localize to the septal pore in rings and pore-centered foci. SPA proteins are not homologous at the primary sequence level but share overall physical properties with intrinsically disordered proteins. Some SPA proteins form aggregates at the septal pore, and in vitro assembly assays suggest aggregation through a nonamyloidal mechanism involving mainly α-helical and disordered structures. SPA loss-of-function phenotypes include excessive septation, septal pore degeneration, and uncontrolled Woronin body activation. Together, our data identify the septal pore as a complex subcellular compartment and focal point for the assembly of unstructured proteins controlling diverse aspects of intercellular connectivity.

Full Text

Duke Authors

Cited Authors

  • Lai, J; Koh, CH; Tjota, M; Pieuchot, L; Raman, V; Chandrababu, KB; Yang, D; Wong, L; Jedd, G

Published Date

  • September 25, 2012

Published In

Volume / Issue

  • 109 / 39

Start / End Page

  • 15781 - 15786

Published By

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.1207467109


  • en