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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.

References associated with 1.Q.1 family:

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. 22955885