Deletion of Smgpi1 encoding a GPI‐anchored protein suppresses sterility of the STRIPAK mutant ΔSmmob3 in the filamentous ascomycete Sordaria macrospora. Issue 4 (26th May 2015)
- Record Type:
- Journal Article
- Title:
- Deletion of Smgpi1 encoding a GPI‐anchored protein suppresses sterility of the STRIPAK mutant ΔSmmob3 in the filamentous ascomycete Sordaria macrospora. Issue 4 (26th May 2015)
- Main Title:
- Deletion of Smgpi1 encoding a GPI‐anchored protein suppresses sterility of the STRIPAK mutant ΔSmmob3 in the filamentous ascomycete Sordaria macrospora
- Authors:
- Frey, Stefan
Lahmann, Yasmine
Hartmann, Thomas
Seiler, Stephan
Pöggeler, Stefanie - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>The <underline>str</underline>iatin <underline>i</underline>nteracting <underline>p</underline>hosphatase <underline>a</underline>nd <underline>k</underline>inase (STRIPAK) complex, which is composed of striatin, protein phosphatase PP2A and kinases, is required for fruiting‐body development and cell fusion in the filamentous ascomycete <italic>S</italic><italic>ordaria macrospora</italic>. Here, we report on the interplay of the <underline>g</underline>lycosyl<underline>p</underline>hosphatidyl<underline>i</underline>nositol (GPI)‐anchored protein SmGPI1 with the kinase activator SmMOB3, a core component of human and fungal STRIPAK complexes. SmGPI1 is conserved among filamentous ascomycetes and was first identified in a yeast two‐hybrid screen using SmMOB3 as bait. The physical interaction of SmMOB3 and SmGPI1 was verified by co‐immunoprecipitation. <italic>In vivo</italic> localization and differential centrifugation revealed that SmGPI1 is predominantly secreted and attached to the cell wall but is also associated with mitochondria and appears to be a dual‐targeted protein. Deletion of <italic>S</italic><italic>mgpi1</italic> led to an increased number of fruiting bodies that were normally shaped but reduced in size. In addition, <italic>S</italic><italic>mmob3</italic> and <italic>S</italic><italic>mgpi1</italic> genetically interact. In the sterile ΔSmmob3 background deletion of<abstract abstract-type="main"> <title>Summary</title> <p>The <underline>str</underline>iatin <underline>i</underline>nteracting <underline>p</underline>hosphatase <underline>a</underline>nd <underline>k</underline>inase (STRIPAK) complex, which is composed of striatin, protein phosphatase PP2A and kinases, is required for fruiting‐body development and cell fusion in the filamentous ascomycete <italic>S</italic><italic>ordaria macrospora</italic>. Here, we report on the interplay of the <underline>g</underline>lycosyl<underline>p</underline>hosphatidyl<underline>i</underline>nositol (GPI)‐anchored protein SmGPI1 with the kinase activator SmMOB3, a core component of human and fungal STRIPAK complexes. SmGPI1 is conserved among filamentous ascomycetes and was first identified in a yeast two‐hybrid screen using SmMOB3 as bait. The physical interaction of SmMOB3 and SmGPI1 was verified by co‐immunoprecipitation. <italic>In vivo</italic> localization and differential centrifugation revealed that SmGPI1 is predominantly secreted and attached to the cell wall but is also associated with mitochondria and appears to be a dual‐targeted protein. Deletion of <italic>S</italic><italic>mgpi1</italic> led to an increased number of fruiting bodies that were normally shaped but reduced in size. In addition, <italic>S</italic><italic>mmob3</italic> and <italic>S</italic><italic>mgpi1</italic> genetically interact. In the sterile ΔSmmob3 background deletion of <italic>S</italic><italic>mgpi1</italic> restores fertility, vegetative growth as well as hyphal‐fusion defects. The suppression effect was specific for the ΔSmmob3 mutant as deletion of <italic>S</italic><italic>mgpi1</italic> in other STRIPAK mutants does not restore fertility.</p> </abstract> … (more)
- Is Part Of:
- Molecular microbiology. Volume 97:Issue 4(2015)
- Journal:
- Molecular microbiology
- Issue:
- Volume 97:Issue 4(2015)
- Issue Display:
- Volume 97, Issue 4 (2015)
- Year:
- 2015
- Volume:
- 97
- Issue:
- 4
- Issue Sort Value:
- 2015-0097-0004-0000
- Page Start:
- 676
- Page End:
- 697
- Publication Date:
- 2015-05-26
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.13054 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3649.xml