MesA, a novel fungal protein required for the stabilization of polarity axes in Aspergillus nidulans

Claire L. Pearson, Kaimei Xu, Kathryn E. Sharpless, Steven D. Harris

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

The Aspergillus nidulans proteome possesses a single formin, SepA, which is required for actin ring formation at septation sites and also plays a role in polarized morphogenesis. Previous observations imply that complex regulatory mechanisms control the function of SepA and ensure its correct localization within hyphal tip cells. To characterize these mechanisms, we undertook a screen for mutations that enhance sepA defects. Of the mutants recovered, mesA1 causes the most dramatic defect in polarity establishment when SepA function is compromised. In a wild-type background, mesA1 mutants undergo aberrant hyphal morphogenesis, whereas septum formation remains unaffected. Molecular characterization revealed that MesA is a novel fungal protein that contains predicted transmembrane domains and localizes to hyphal tips. We show that MesA promotes the localized assembly of actin cables at polarization sites by facilitating the stable recruitment of SepA. We also provide evidence that MesA may regulate the formation or distribution of sterol-rich membrane domains. Our results suggest that these domains may be part of novel mechanism that directs SepA to hyphal tips.

Original languageEnglish (US)
Pages (from-to)3658-3672
Number of pages15
JournalMolecular biology of the cell
Volume15
Issue number8
DOIs
StatePublished - Aug 1 2004

Fingerprint

Aspergillus nidulans
Fungal Proteins
Morphogenesis
Actins
Sterols
Proteome
Mutation
Membranes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

MesA, a novel fungal protein required for the stabilization of polarity axes in Aspergillus nidulans. / Pearson, Claire L.; Xu, Kaimei; Sharpless, Kathryn E.; Harris, Steven D.

In: Molecular biology of the cell, Vol. 15, No. 8, 01.08.2004, p. 3658-3672.

Research output: Contribution to journalArticle

Pearson, Claire L. ; Xu, Kaimei ; Sharpless, Kathryn E. ; Harris, Steven D. / MesA, a novel fungal protein required for the stabilization of polarity axes in Aspergillus nidulans. In: Molecular biology of the cell. 2004 ; Vol. 15, No. 8. pp. 3658-3672.
@article{452556d2e9a14b958b5c345a3c67f573,
title = "MesA, a novel fungal protein required for the stabilization of polarity axes in Aspergillus nidulans",
abstract = "The Aspergillus nidulans proteome possesses a single formin, SepA, which is required for actin ring formation at septation sites and also plays a role in polarized morphogenesis. Previous observations imply that complex regulatory mechanisms control the function of SepA and ensure its correct localization within hyphal tip cells. To characterize these mechanisms, we undertook a screen for mutations that enhance sepA defects. Of the mutants recovered, mesA1 causes the most dramatic defect in polarity establishment when SepA function is compromised. In a wild-type background, mesA1 mutants undergo aberrant hyphal morphogenesis, whereas septum formation remains unaffected. Molecular characterization revealed that MesA is a novel fungal protein that contains predicted transmembrane domains and localizes to hyphal tips. We show that MesA promotes the localized assembly of actin cables at polarization sites by facilitating the stable recruitment of SepA. We also provide evidence that MesA may regulate the formation or distribution of sterol-rich membrane domains. Our results suggest that these domains may be part of novel mechanism that directs SepA to hyphal tips.",
author = "Pearson, {Claire L.} and Kaimei Xu and Sharpless, {Kathryn E.} and Harris, {Steven D.}",
year = "2004",
month = "8",
day = "1",
doi = "10.1091/mbc.E03-11-0803",
language = "English (US)",
volume = "15",
pages = "3658--3672",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "8",

}

TY - JOUR

T1 - MesA, a novel fungal protein required for the stabilization of polarity axes in Aspergillus nidulans

AU - Pearson, Claire L.

AU - Xu, Kaimei

AU - Sharpless, Kathryn E.

AU - Harris, Steven D.

PY - 2004/8/1

Y1 - 2004/8/1

N2 - The Aspergillus nidulans proteome possesses a single formin, SepA, which is required for actin ring formation at septation sites and also plays a role in polarized morphogenesis. Previous observations imply that complex regulatory mechanisms control the function of SepA and ensure its correct localization within hyphal tip cells. To characterize these mechanisms, we undertook a screen for mutations that enhance sepA defects. Of the mutants recovered, mesA1 causes the most dramatic defect in polarity establishment when SepA function is compromised. In a wild-type background, mesA1 mutants undergo aberrant hyphal morphogenesis, whereas septum formation remains unaffected. Molecular characterization revealed that MesA is a novel fungal protein that contains predicted transmembrane domains and localizes to hyphal tips. We show that MesA promotes the localized assembly of actin cables at polarization sites by facilitating the stable recruitment of SepA. We also provide evidence that MesA may regulate the formation or distribution of sterol-rich membrane domains. Our results suggest that these domains may be part of novel mechanism that directs SepA to hyphal tips.

AB - The Aspergillus nidulans proteome possesses a single formin, SepA, which is required for actin ring formation at septation sites and also plays a role in polarized morphogenesis. Previous observations imply that complex regulatory mechanisms control the function of SepA and ensure its correct localization within hyphal tip cells. To characterize these mechanisms, we undertook a screen for mutations that enhance sepA defects. Of the mutants recovered, mesA1 causes the most dramatic defect in polarity establishment when SepA function is compromised. In a wild-type background, mesA1 mutants undergo aberrant hyphal morphogenesis, whereas septum formation remains unaffected. Molecular characterization revealed that MesA is a novel fungal protein that contains predicted transmembrane domains and localizes to hyphal tips. We show that MesA promotes the localized assembly of actin cables at polarization sites by facilitating the stable recruitment of SepA. We also provide evidence that MesA may regulate the formation or distribution of sterol-rich membrane domains. Our results suggest that these domains may be part of novel mechanism that directs SepA to hyphal tips.

UR - http://www.scopus.com/inward/record.url?scp=3342893961&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=3342893961&partnerID=8YFLogxK

U2 - 10.1091/mbc.E03-11-0803

DO - 10.1091/mbc.E03-11-0803

M3 - Article

C2 - 15155805

AN - SCOPUS:3342893961

VL - 15

SP - 3658

EP - 3672

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 8

ER -