1.Q.1.  The Fungal Septal Pore (FSP) Family 

Multicellular fungi possess cell-to-cell channels (septal pores) that allow intercellular communication and transport. Using a combination of MS of Woronin body-associated proteins and a bioinformatics approach that identifies related proteins based on composition and character, Lai et al. 2012 identified 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. The data of   Lai et al. 2012 identified the septal pore as a complex subcellular compartment and focal point for the assembly of unstructured proteins controlling diverse aspects of intercellular connectivity.



Lai, J., C.H. Koh, M. Tjota, L. Pieuchot, V. Raman, K.B. Chandrababu, D. Yang, L. Wong, and G. Jedd. (2012). Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity. Proc. Natl. Acad. Sci. USA 109: 15781-15786.


TC#NameOrganismal TypeExample

Septal pore-associated proteins, SPA1 - 18 (Lai et al. 2012).

SPA1 - 18 of Neurospora crassa
SPA1, 569 aas
SPA2, 763 aas
SPA3, 1055 aas
SPA4, 856 aas
SPA5, 1015 aas
SPA6, 584 aas
SPA7, 722 aas
SPA8, 598 aas
SPA9, 1348 aas
SPA10, 1752 aas (Dap-1)
SPA11, 524 aas
SPA12, 1200 aas
SPA13, 1229 aas
SPA14, 770 aas
SPA15, 1401 aas
SPA16, 792 aas
SPA17, 386 aas
SPA18, 1117 aas