Functional characterization of the pleckstrin homology domain of a cellulose synthase from the oomycete Saprolegnia monoica

Johanna Fugelstad, Christian Brown, Elvira Hukasova, Gustav Sundqvist, Arne Lindqvist, Vincent Bulone

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8 Citations (Scopus)


Some oomycetes, for instance Saprolegnia parasitica, are severe fish pathogens that cause important economic losses worldwide. Cellulose biosynthesis is a vital process for this class of microorganisms, but the corresponding molecular mechanisms are poorly understood. Of all cellulose synthesizing enzymes known, only some oomycete cellulose synthases contain a pleckstrin homology (PH) domain. Some human PH domains bind specifically to phosphoinositides, but most PH domains bind phospholipids in a non-specific manner. In addition, some PH domains interact with various proteins. Here we have investigated the function of the PH domain of cellulose synthase 2 from the oomycete Saprolegnia monoica (SmCesA2), a species closely related to S. parasitica. The SmCesA2 PH domain is similar to the C-terminal PH domain of the human protein TAPP1. It binds in vitro to phosphoinositides, F-actin and microtubules, and co-localizes with F-actin in vivo. Our results suggest a role of the SmCesA2 PH domain in the regulation, trafficking and/or targeting of the cell wall synthesizing enzyme.

Original languageEnglish
Pages (from-to)1248-1253
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 27 Jan 2012
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by grant #2009-515 from the Swedish Research Council Formas to V.B. The funding agency had no involvement in study design, data collection, analysis and interpretation, and in the writing and submission of the manuscript. The authors declare no conflicts of interest.


  • Cell wall biosynthesis
  • Cellulose synthase
  • F-actin
  • Oomycetes
  • Phosphoinositides
  • Pleckstrin homology domain


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