Please use this identifier to cite or link to this item: https://doi.org/10.1073/pnas.1207467109
Title: Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity
Authors: Lai, J.
Koh, C.H.
Tjota, M.
Pieuchot, L.
Raman, V.
Chandrababu, K.B.
Yang, D. 
Wong, L. 
Jedd, G.
Keywords: Filamentous fungus
Multicellular organization
Neurospora crassa
Issue Date: 2012
Source: Lai, J., Koh, C.H., Tjota, M., Pieuchot, L., Raman, V., Chandrababu, K.B., Yang, D., Wong, L., Jedd, G. (2012). Intrinsically disordered proteins aggregate at fungal cell-to-cell channels and regulate intercellular connectivity. Proceedings of the National Academy of Sciences of the United States of America 109 (39) : 15781-15786. ScholarBank@NUS Repository. https://doi.org/10.1073/pnas.1207467109
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 á-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.
Source Title: Proceedings of the National Academy of Sciences of the United States of America
URI: http://scholarbank.nus.edu.sg/handle/10635/43118
ISSN: 00278424
DOI: 10.1073/pnas.1207467109
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

29
checked on Dec 11, 2017

WEB OF SCIENCETM
Citations

28
checked on Dec 11, 2017

Page view(s)

59
checked on Dec 9, 2017

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.