Elramli, Nadia and Karahoda, Betim and Bayram, Ozlem Sarikaya and Frawley, Dean and Ulas, Mevlut and Oakley, C. Elizabeth and Oakley, Berl and Seiler, Stephan and Bayram, Ozgur
(2019)
Assembly of a heptameric STRIPAK complex is required for coordination of light-dependent multicellular fungal development with secondary metabolism in Aspergillus nidulans.
PLos Genetics, 15 (3).
e1008053.
ISSN 1553-7390
Abstract
Eukaryotic striatin forms striatin-interacting phosphatase and kinase (STRIPAK) complexes that control many cellular processes including development, cellular transport, signal transduction, stem cell differentiation and cardiac functions. However, detailed knowledge of complex assembly and its roles in stress responses are currently poorly understood. Here, we discovered six striatin (StrA) interacting proteins (Sips), which form a heptameric complex in the filamentous fungus Aspergillus nidulans. The complex consists of the striatin scaffold StrA, the Mob3-type kinase coactivator SipA, the SIKE-like protein SipB, the STRIP1/2 homolog SipC, the SLMAP-related protein SipD and the catalytic and regulatory phosphatase 2A subunits SipE (PpgA), and SipF, respectively. Single and double deletions of the complex components result in loss of multicellular light-dependent fungal development, secondary metabolite production (e.g. mycotoxin Sterigmatocystin) and reduced stress responses. sipA (Mob3) deletion is epistatic to strA deletion by supressing all the defects caused by the lack of striatin. The STRIPAK complex, which is established during vegetative growth and maintained during the early hours of light and dark development, is mainly formed on the nuclear envelope in the presence of the scaffold StrA. The loss of the scaffold revealed three STRIPAK subcomplexes: (I) SipA only interacts with StrA, (II) SipB-SipD is found as a heterodimer, (III) SipC, SipE and SipF exist as a heterotrimeric complex. The STRIPAK complex is required for proper expression of the heterotrimeric VeA-VelB-LaeA complex which coordinates fungal development and secondary metabolism. Furthermore, the STRIPAK complex modulates two important MAPK pathways by promoting phosphorylation of MpkB and restricting nuclear shuttling of MpkC in the absence of stress conditions. SipB in A. nidulans is similar to human suppressor of IKK-ε(SIKE) protein which supresses antiviral responses in mammals, while velvet family proteins show strong similarity to mammalian proinflammatory NF-KB proteins. The presence of these proteins in A. nidulans further strengthens the hypothesis that mammals and fungi use similar proteins for their immune response and secondary metabolite production, respectively.
Item Type: |
Article
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Additional Information: |
© 2019 Elramli et al. This is an open
access article distributed under the terms of the
Creative Commons Attribution License, which
permits unrestricted use, distribution, and
reproduction in any medium, provided the original
author and source are credited. Citation: Elramli N, Karahoda B, Sarikaya-Bayram O, Frawley D, Ulas M, Oakley CE, et al. (2019)
Assembly of a heptameric STRIPAK complex is
required for coordination of light-dependent
multicellular fungal development with secondary
metabolism in Aspergillus nidulans. PLoS Genet 15
(3): e1008053. https://doi.org/10.1371/journal.
pgen.1008053 |
Keywords: |
Assembly; heptameric STRIPAK complex; light-dependent
multicellular fungal development;
secondary metabolism; Aspergillus nidulans; |
Academic Unit: |
Faculty of Science and Engineering > Biology |
Item ID: |
10654 |
Identification Number: |
https://doi.org/10.1371/journal.pgen.1008053 |
Depositing User: |
Ozlem Sarikaya Bayram
|
Date Deposited: |
27 Mar 2019 12:02 |
Journal or Publication Title: |
PLos Genetics |
Publisher: |
Public Library of Science |
Refereed: |
Yes |
URI: |
|
Use Licence: |
This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available
here |
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