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Septin phosphorylation and coiled-coil domains function in cell and septin ring morphology in the filamentous fungus Ashbya gossypii.

Publication ,  Journal Article
Meseroll, RA; Occhipinti, P; Gladfelter, AS
Published in: Eukaryot Cell
February 2013

Septins are a class of GTP-binding proteins conserved throughout many eukaryotes. Individual septin subunits associate with one another and assemble into heteromeric complexes that form filaments and higher-order structures in vivo. The mechanisms underlying the assembly and maintenance of higher-order structures in cells remain poorly understood. Septins in several organisms have been shown to be phosphorylated, although precisely how septin phosphorylation may be contributing to the formation of high-order septin structures is unknown. Four of the five septins expressed in the filamentous fungus, Ashbya gossypii, are phosphorylated, and we demonstrate here the diverse roles of these phosphorylation sites in septin ring formation and septin dynamics, as well as cell morphology and viability. Intriguingly, the alteration of specific sites in Cdc3p and Cdc11p leads to a complete loss of higher-order septin structures, implicating septin phosphorylation as a regulator of septin structure formation. Introducing phosphomimetic point mutations to specific sites in Cdc12p and Shs1p causes cell lethality, highlighting the importance of normal septin modification in overall cell function and health. In addition to discovering roles for phosphorylation, we also present diverse functions for conserved septin domains in the formation of septin higher-order structure. We previously showed the requirement for the Shs1p coiled-coil domain in limiting septin ring size and reveal here that, in contrast to Shs1p, the coiled-coil domains of Cdc11p and Cdc12p are required for septin ring formation. Our results as a whole reveal novel roles for septin phosphorylation and coiled-coil domains in regulating septin structure and function.

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Published In

Eukaryot Cell

DOI

EISSN

1535-9786

Publication Date

February 2013

Volume

12

Issue

2

Start / End Page

182 / 193

Location

United States

Related Subject Headings

  • Septins
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Protein Processing, Post-Translational
  • Phosphorylation
  • Mutagenesis, Site-Directed
  • Microscopy, Fluorescence
  • Microbiology
  • Microbial Viability
 

Citation

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Meseroll, R. A., Occhipinti, P., & Gladfelter, A. S. (2013). Septin phosphorylation and coiled-coil domains function in cell and septin ring morphology in the filamentous fungus Ashbya gossypii. Eukaryot Cell, 12(2), 182–193. https://doi.org/10.1128/EC.00251-12
Meseroll, Rebecca A., Patricia Occhipinti, and Amy S. Gladfelter. “Septin phosphorylation and coiled-coil domains function in cell and septin ring morphology in the filamentous fungus Ashbya gossypii.Eukaryot Cell 12, no. 2 (February 2013): 182–93. https://doi.org/10.1128/EC.00251-12.
Meseroll, Rebecca A., et al. “Septin phosphorylation and coiled-coil domains function in cell and septin ring morphology in the filamentous fungus Ashbya gossypii.Eukaryot Cell, vol. 12, no. 2, Feb. 2013, pp. 182–93. Pubmed, doi:10.1128/EC.00251-12.

Published In

Eukaryot Cell

DOI

EISSN

1535-9786

Publication Date

February 2013

Volume

12

Issue

2

Start / End Page

182 / 193

Location

United States

Related Subject Headings

  • Septins
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Structure, Quaternary
  • Protein Processing, Post-Translational
  • Phosphorylation
  • Mutagenesis, Site-Directed
  • Microscopy, Fluorescence
  • Microbiology
  • Microbial Viability