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The role of actin, fimbrin and endocytosis in growth of hyphae in Aspergillus nidulans
"... Filamentous fungi are ideal systems to study the process of polarized growth, as their life cycle is dominated by hyphal growth exclusively at the cell apex. The actin cytoskeleton plays an important role in this growth. Until now, there have been no tools to visualize actin or the actin-binding pro ..."
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Filamentous fungi are ideal systems to study the process of polarized growth, as their life cycle is dominated by hyphal growth exclusively at the cell apex. The actin cytoskeleton plays an important role in this growth. Until now, there have been no tools to visualize actin or the actin-binding protein fimbrin in live cells of a filamentous fungus. We investigated the roles of actin (ActA) and fimbrin (FimA) in hyphal growth in Aspergillus nidulans. We examined the localization of ActA::GFP and FimA::GFP in live cells, and each displayed a similar localization pattern. In actively growing hyphae, cortical ActA::GFP and FimA::GFP patches were highly mobile throughout the hypha and were concentrated near hyphal apices. A patch-depleted zone occupied the apical 0.5 mm of growing hypha. Both FimA::GFP and Act::GFP also localize transiently to septa. Movement and later localization of both was compromised after cytocha-lasin treatment. Disruption of fimA resulted in delayed polarity establishment during conidium germination, abnormal hyphal growth and endocytosis defects in apolar cells. Endocytosis was severely impaired in apolar fimA disruption cells. Our data support a novel apical recycling model which indicates a critical role for actin patch-mediated endocytosis to maintain polarized growth at the apex.
Role of Actin Cytoskeletal Dynamics in Activation of the Cyclic AMP Pathway and HWP1 Gene Expression in Candida albicans � †
, 2007
"... This article cites 78 articles, 51 of which can be accessed free ..."
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This article cites 78 articles, 51 of which can be accessed free
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"... Structural characteristics affecting functions of two actin regulating proteins ..."
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Structural characteristics affecting functions of two actin regulating proteins
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, 2008
"... The S. cerevisisae Rho GTPase Cdc42p localizes around the entire plasma membrane, but is only activated at sites of polarized growth in a cell cycle-dependent manner. This spatial and temporal control ensures that Cdc42p is inactive within the cytoplasm and outside of the polarized cortical domain, ..."
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The S. cerevisisae Rho GTPase Cdc42p localizes around the entire plasma membrane, but is only activated at sites of polarized growth in a cell cycle-dependent manner. This spatial and temporal control ensures that Cdc42p is inactive within the cytoplasm and outside of the polarized cortical domain, and is active at sites of polarized growth. This dissertation addresses spatial control of Cdc42p by examining complex formation with its sole guanine nucleotide dissociation inhibitor (GDI) Rdi1p and its sole guanine nucleotide exchange factor (GEF) Cdc24p. Rdi1p is not essential; however, when overexpressed, it is lethal, suggesting that it does have an important negative regulatory function. To study complex formation and localization, the technique of bimolecular fluorescence complementation (BiFC) was used to study in vivo Rdi1p-Cdc42p complex formation and localization, and how mutations to Rdi1p’s two functional domains, the regulatory arm and the geranylgeranyl binding pocket, affected the complex. Rdi1p and Cdc42p interacted diffusely throughout the cytoplasm of
Correspondence
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Re-use of this article is permitted in accordance with the Terms and Conditions set out at
Executive Summary
, 2010
"... A discussion on implementation of global equity allocation and evolving mandate structures ..."
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A discussion on implementation of global equity allocation and evolving mandate structures
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, 2015
"... d The activity of ADF/cofilin depends on actin network architecture d Aip1 rapidly and completely disassembles actin networks marked by ADF/cofilin d 23 ADF/cofilins create mechanical stress and sever individual actin filaments d Aip1 stochastically disassembles filaments decorated with ..."
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d The activity of ADF/cofilin depends on actin network architecture d Aip1 rapidly and completely disassembles actin networks marked by ADF/cofilin d 23 ADF/cofilins create mechanical stress and sever individual actin filaments d Aip1 stochastically disassembles filaments decorated with
Actin-Filament Stochastic Mediated by ADF/Cofilin
"... aments by ADF/cofilin is the key mechanism modulating treadmilling comprises the addition of actin monomers the prominent and frequent shortening events. The net effect of continuous actin polymerization, driven by a processive formin that uses profilin-actin, and of at filament barbed ends and the ..."
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aments by ADF/cofilin is the key mechanism modulating treadmilling comprises the addition of actin monomers the prominent and frequent shortening events. The net effect of continuous actin polymerization, driven by a processive formin that uses profilin-actin, and of at filament barbed ends and the accompanying depoly-merization of actin subunits at filament pointed ends (rate of 0.27 s21 [8]). This is two orders of magnitude too slow for it to be compatible with cell locomotion [9]. Biomimetic systems that reconstitute actin-based motility in vitro are a valuable tool for identifying the min-imum set of actin-binding proteins required for generat-
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"... rC mins are autoinhibited by association of their N- and C-terminalvents both formin nucleation and processive barbed end elongation and decreases formin’s affinity for the barbed end. Furthermore, low micromolar concen-trations of SMIFH2 disrupt formin-dependent, but not Arp2/3 complex-dependent, a ..."
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rC mins are autoinhibited by association of their N- and C-terminalvents both formin nucleation and processive barbed end elongation and decreases formin’s affinity for the barbed end. Furthermore, low micromolar concen-trations of SMIFH2 disrupt formin-dependent, but not Arp2/3 complex-dependent, actin cytoskeletal structures in fission yeast and mammalian NIH 3T3 fibroblasts.
