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Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus.

Publication ,  Journal Article
Juvvadi, PR; Belina, D; Soderblom, EJ; Moseley, MA; Steinbach, WJ
Published in: Biochem Biophys Res Commun
February 15, 2013

We previously analyzed the differential localization patterns of five septins (AspA-E), including a filamentous fungal-specific septin, AspE, in the human pathogen Aspergillus fumigatus. Here we utilized the A. fumigatus strain expressing an AspE-EGFP fusion protein and show that this novel septin with a tubular localization pattern in hyphae is phosphorylated in vivo and interacts with the other septins, AspA, AspB, AspC and AspD. The other major proteins interacting with AspE included the cytoskeletal proteins, actin and tubulin, which may be involved in the organization and transport of the septins. This is the first report analyzing the phosphorylation of AspE and localizing the sites of phosphorylation, and opens opportunities for further analysis on the role of post-translational modifications in the assembly and organization of A. fumigatus septins. This study also describes the previously unknown interaction of AspE with the actin-microtubule network. Furthermore, the novel GFP-Trap® affinity purification method used here complements widely-used GFP localization studies in fungal systems.

Duke Scholars

Published In

Biochem Biophys Res Commun

DOI

EISSN

1090-2104

Publication Date

February 15, 2013

Volume

431

Issue

3

Start / End Page

547 / 553

Location

United States

Related Subject Headings

  • Tubulin
  • Septins
  • Protein Structure, Tertiary
  • Protein Processing, Post-Translational
  • Phosphorylation
  • Molecular Sequence Data
  • Humans
  • Green Fluorescent Proteins
  • Conserved Sequence
  • Biochemistry & Molecular Biology
 

Citation

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Juvvadi, P. R., Belina, D., Soderblom, E. J., Moseley, M. A., & Steinbach, W. J. (2013). Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus. Biochem Biophys Res Commun, 431(3), 547–553. https://doi.org/10.1016/j.bbrc.2013.01.020
Juvvadi, Praveen Rao, Detti Belina, Erik J. Soderblom, M Arthur Moseley, and William J. Steinbach. “Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus.Biochem Biophys Res Commun 431, no. 3 (February 15, 2013): 547–53. https://doi.org/10.1016/j.bbrc.2013.01.020.
Juvvadi PR, Belina D, Soderblom EJ, Moseley MA, Steinbach WJ. Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus. Biochem Biophys Res Commun. 2013 Feb 15;431(3):547–53.
Juvvadi, Praveen Rao, et al. “Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus.Biochem Biophys Res Commun, vol. 431, no. 3, Feb. 2013, pp. 547–53. Pubmed, doi:10.1016/j.bbrc.2013.01.020.
Juvvadi PR, Belina D, Soderblom EJ, Moseley MA, Steinbach WJ. Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus. Biochem Biophys Res Commun. 2013 Feb 15;431(3):547–553.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

EISSN

1090-2104

Publication Date

February 15, 2013

Volume

431

Issue

3

Start / End Page

547 / 553

Location

United States

Related Subject Headings

  • Tubulin
  • Septins
  • Protein Structure, Tertiary
  • Protein Processing, Post-Translational
  • Phosphorylation
  • Molecular Sequence Data
  • Humans
  • Green Fluorescent Proteins
  • Conserved Sequence
  • Biochemistry & Molecular Biology