The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics

Han, Gongshe; Liu, Bo; Zhang, Jun; Zuo, Wenqi; Morris, Nicholas P.; Xiang, Xin

doi:10.1016/s0960-9822(01)00200-7

Cited by 177 publications

(226 citation statements)

References 25 publications

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“…The available evidence suggests that they are involved in long-range transport of vesicles to the hyphal tip region (Horio and Oakley, 2005, and other data discussed therein; Lenz et al, 2006). Note that there is considerable evidence that microtubules are extremely dynamic at the hyphal tip (Han et al, 2001;Szewczyk, Symeonidou-Sideris, and Oakley, unpublished data), continually growing and shrinking. They are thus not in stable contact with the Spitzenkö rper and vesicles probably fall off of microtubules in the tip area more often than they are delivered directly to the Spitzenkö rper.…”

Section: Functions Of Cytoskeletal Elementsmentioning

confidence: 87%

The Tip Growth Apparatus ofAspergillus nidulans

Taheri-Talesh

Horio

Araújo‐Bazán

et al. 2008

MBoC

273

414

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Hyphal tip growth in fungi is important because of the economic and medical importance of fungi, and because it may be a useful model for polarized growth in other organisms. We have investigated the central questions of the roles of cytoskeletal elements and of the precise sites of exocytosis and endocytosis at the growing hyphal tip by using the model fungus Aspergillus nidulans. Time-lapse imaging of fluorescent fusion proteins reveals a remarkably dynamic, but highly structured, tip growth apparatus. Live imaging of SYNA, a synaptobrevin homologue, and SECC, an exocyst component, reveals that vesicles accumulate in the Spitzenkö rper (apical body) and fuse with the plasma membrane at the extreme apex of the hypha. SYNA is recycled from the plasma membrane by endocytosis at a collar of endocytic patches, 1-2 m behind the apex of the hypha, that moves forward as the tip grows. Exocytosis and endocytosis are thus spatially coupled. Inhibitor studies, in combination with observations of fluorescent fusion proteins, reveal that actin functions in exocytosis and endocytosis at the tip and in holding the tip growth apparatus together. Microtubules are important for delivering vesicles to the tip area and for holding the tip growth apparatus in position. INTRODUCTIONPolarized cell growth occurs in most eukaryotic phyla, and it includes a plethora of important phenomena, such as neuronal growth cone extension in animals and pollen tube extension in vascular plants. It is particularly important in filamentous fungi where nearly all growth occurs by hyphal tip extension (reviewed by Momany, 2002). Given that some filamentous fungi are important fermentation organisms, the growth of which is of considerable economic importance, whereas others are serious plant, animal, and human pathogens, there is considerable interest in the mechanisms of tip growth in these organisms.A great deal of progress has been made in understanding fungal tip growth (summarized by Harris et al., 2005; Steinberg, 2007a,b;Riquelme et al., 2007), but key questions remain unanswered. There is general agreement that fungal tip growth involves the synthesis of cell wall components in the cell body, the incorporation of these components into vesicles, the transport of these vesicles to the cell tip, the fusion of these vesicles with the plasma membrane in the area of the cell tip (exocytosis) to release their contents, and the cross-linking of the components after release. It is clear that both microtubules and actin microfilaments play important roles in fungal tip growth, but their exact functions are not yet defined. The exact sites of exocytosis and endocytosis also remain to be determined. The positions of the site(s) of exocytosis are particularly important because fungal walls are relatively stiff structures, and once they have formed the shape of the hypha is established. Hyphal shape is thus determined to a very significant extent by where the wall precursors are released from the cytoplasm, i.e., by the positioning of the site(s) of exocyto...

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Section: Functions Of Cytoskeletal Elementsmentioning

confidence: 87%

The Tip Growth Apparatus ofAspergillus nidulans

Taheri-Talesh

Horio

Araújo‐Bazán

et al. 2008

MBoC

273

414

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“…Spindle orientation was also disturbed in several cells, regardless of whether the nucleus was in the mother yeast cell or in the filament. Filaments that survived after 24 h of CaCDC5 repression contained extensive cytoplasmic microtubule arrays resembling those in serum-induced hyphae of Candida ( Figure 4C) and hyphae of other filamentous fungi (Han et al, 2001;Hazan et al, 2002), although the intensity of the Tub1p-GFP signal was greater in CaCdc5p-depleted cells at 30°C compared with serum-induced hyphae at 37°C. The remaining dead cells either did not stain or contained a diffuse signal.…”

Section: Cacdc5p Is Required For Spindle Elongationmentioning

confidence: 94%

Depletion of a Polo-like Kinase inCandida albicansActivates Cyclase-dependent Hyphal-like Growth

Bachewich

Thomas²,

Whiteway³

2003

MBoC

133

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Morphogenesis in the fungal pathogen Candida albicans is an important virulence-determining factor, as a dimorphic switch between yeast and hyphal growth forms can increase pathogenesis. We identified CaCDC5, a cell cycle regulatory polo-like kinase (PLK) in C. albicans and demonstrate that shutting off its expression induced cell cycle defects and dramatic changes in morphology. Cells lacking CaCdc5p were blocked early in nuclear division with very short spindles and unseparated chromatin. GFP-tagged CaCdc5p localized to unseparated spindle pole bodies, the spindle, and chromatin, consistent with a role in spindle elongation at an earlier point in the cell cycle than that described for the homologue Cdc5p in yeast. Strikingly, the cell cycle defects were accompanied by the formation of hyphal-like filaments under yeast growth conditions. Filament growth was determinate, as the filaments started to die after 24 h. The filaments resembled serum-induced hyphae with respect to morphology, organization of cytoplasmic microtubules, localization of nuclei, and expression of hyphal-specific components. Filament formation required CaCDC35, but not EFG1 or CPH1. Similar defects in spindle elongation and a corresponding induction of filaments occurred when yeast cells were exposed to hydroxyurea. Because CaCdc5p does not appear to act as a direct repressor of hyphal growth, the data suggest that a target of CaCdc5p function is associated with hyphal-like development. Thus, an internal, cell cycle-related cue can activate hyphal regulatory networks in Candida.

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“…LIS1, encoded by the gene the mutation in which is associated with the type I lissencephaly, 16,17 has been defined as a major cellular interactor of 3A. LIS1 was previously shown to be involved in the dynein motor complex that determines microtubule-associated movement of organelles and membrane vesicles [18][19][20][21][22][23][24][25][26] and maintenance of the integrity of the Golgi apparatus and juxta-centrosomal distribution of its membranes (reviewed in refs. [27][28][29][30][31][32][33][34][35].…”

Section: Introductionmentioning

confidence: 99%

Poliovirus Protein 3A Binds and Deregulates LIS1, Causing Block of Membrane Protein Trafficking and Deregulation of Cell Division

Kondratova¹,

Neznanov²,

Kondratov³

et al. 2005

Cell Cycle

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Many viruses encode anti-apoptotic proteins that have been used as valuable tools for identification and analysis of key cellular regulators of programmed cell death. Here we demonstrate that the poliovirus protein 3A, previously shown to exhibit anti-apoptotic activity, binds and inactivates LIS1, a component of the dynein/dynactin motor complex, encoded by the gene mutated in patients with type I lissencephaly ("smooth brain"), thereby causing deregulation of endoplasmatic reticilum-to-Golgi vesicular transport, resulting in rapid disappearance of short-living receptors from the plasma membrane and loss of cell sensitivity to TNF and interferon. Truncated derivatives of LIS1, acting in a dominant negative manner, cause similar effects. However, 3A, being an endoplasmic reticulumbound protein, locks Golgi-targeted YFP in the endoplasmatic reticilum, while expression of LIS1 mutants results in a dispersed cytoplasmic localization of the reporter protein. LIS1 dysfunction caused by ectopic expressing 3A or LIS1 mutants, as well as by overexpression of wild type LIS1, leads to cell blocking at the postmitotic stage associated with inability to undergo cytokinesis. Thus, the use of poliovirus protein as a research tool allowed us to reveal the role of cellular protein LIS1 in membrane protein trafficking, maintenance of Golgi integrity, surface presentation of unstable receptors, cell sensitivity to TNF-induced apoptosis and cell cycle progression.

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The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics

Cited by 177 publications

References 25 publications

The Tip Growth Apparatus ofAspergillus nidulans

The Tip Growth Apparatus ofAspergillus nidulans

Depletion of a Polo-like Kinase inCandida albicansActivates Cyclase-dependent Hyphal-like Growth

Poliovirus Protein 3A Binds and Deregulates LIS1, Causing Block of Membrane Protein Trafficking and Deregulation of Cell Division

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