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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Juvvadi, PR; Belina, D; Soderblom, EJ; Moseley, MA; Steinbach, WJ

Published Date

  • February 15, 2013

Published In

Volume / Issue

  • 431 / 3

Start / End Page

  • 547 - 553

PubMed ID

  • 23321313

Pubmed Central ID

  • PMC3587984

Electronic International Standard Serial Number (EISSN)

  • 1090-2104

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2013.01.020


  • eng

Conference Location

  • United States