title: Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity.
abstract: 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.
authors.affiliation: Temasek Life Sciences Laboratory, National University of Singapore, Singapore.
authors.forename: Julian
authors.initials: J
authors.lastname: Lai
authors.forename: Chuan Hock
authors.initials: CH
authors.lastname: Koh
authors.forename: Monika
authors.initials: M
authors.lastname: Tjota
authors.forename: Laurent
authors.initials: L
authors.lastname: Pieuchot
authors.forename: Vignesh
authors.initials: V
authors.lastname: Raman
authors.forename: Karthik Balakrishna
authors.initials: KB
authors.lastname: Chandrababu
authors.forename: Daiwen
authors.initials: D
authors.lastname: Yang
authors.forename: Limsoon
authors.initials: L
authors.lastname: Wong
authors.forename: Gregory
authors.initials: G
authors.lastname: Jedd
mesh_terms: D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism*; D009492:Neurospora crassa / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D017433:Protein Structure, Secondary
chemical_list: D005656:Fungal Proteins; D046912:Multiprotein Complexes