Nuclear migration advances in fungi

Morris, Nicholas P.; Xiang, Xin; Beckwith, Susan M.

doi:10.1016/s0962-8924(00)89039-x

Cited by 87 publications

(18 citation statements)

References 37 publications

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“…Alternatively, the 8-kD CDLC might be involved in anchoring the dynein/dynactin complex to the hyphal tip. Whatever the mechanism, our results are consistent with a model in which cortically anchored dynein moves nuclei by pulling on astral MTs attached to nuclei ( Palmer et al, 1992 ; Plamann et al, 1994 ; Morris et al, 1995 ; Carminati and Stearns, 1998 ; Efimov and Morris, 1998 ). However, it is important to recognize that they by no means prove the model.…”

Section: Discussionsupporting

confidence: 89%

“…Morris, unpublished observations). These observations support but by no means prove a class of models in which nuclei are moved in filamentous fungi by the interaction between cortically fixed dynein/dynactin and SPB microtubules ( Plamann et al, 1994 ; Morris et al, 1995 ; Carminati and Stearns, 1998 ; Efimov and Morris, 1998 ). Presumably, dynein, which is a minus end–directed motor, moves nuclei by attempting to migrate along SPB MTs toward the SPB microtubule organizing center, thereby reeling in the nucleus.…”

mentioning

confidence: 91%

“…In higher eukaryotes, nuclear migration plays a significant role in a wide variety of processes, which include epithelial folding ( Sauer, 1935 ; Schoenwolf and Smith, 1990 ; Viebahn et al, 1995 ), cancer cell migration ( Klominek et al, 1991 ), pronuclear migration during fertilization ( Schatten, 1982 ; Reinsch and Karsenti, 1997 ), nuclear corticalization in insect eggs ( Zalokar and Erk, 1976 ; Baker et al, 1993 ), mitotic spindle orientation in Drosophila ( McGrail and Hays, 1997 ; Theurkauf, 1997 ), and development of the Drosophila eye ( Fan and Ready, 1997 ). Among lower eukaryotes, nuclear migration is required to distribute nuclei through the hyphal mycelium in filamentous fungi (reviewed by Morris et al, 1995 ), to move daughter nuclei into the bud in budding yeast (reviewed by Hoyt et al, 1997 ; Stearns, 1997 ), to partition nuclei into daughter cells in fission yeast (reviewed by Hagan and Yanagida, 1997 ) and for karyogamy (reviewed by Rose, 1996 ). In the budding yeast Saccharomyces cerevisiae , cytoplasmic dynein, dynactin, and a set of kinesins play overlapping roles in nuclear positioning and migration into the bud.…”

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confidence: 99%

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The “8-kD” Cytoplasmic Dynein Light Chain Is Required for Nuclear Migration and for Dynein Heavy Chain Localization in Aspergillus nidulans

Beckwith¹,

Roghi²,

Liu³

et al. 1998

The Journal of Cell Biology

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The heavy chain of cytoplasmic dynein is required for nuclear migration in Aspergillus nidulans and other fungi. Here we report on a new gene required for nuclear migration, nudG, which encodes a homologue of the “8-kD” cytoplasmic dynein light chain (CDLC). We demonstrate that the temperature sensitive nudG8 mutation inhibits nuclear migration and growth at restrictive temperature. This mutation also inhibits asexual and sexual sporulation, decreases the intracellular concentration of the nudG CDLC protein and causes the cytoplasmic dynein heavy chain to be absent from the mycelial tip, where it is normally located in wild-type mycelia. Coimmunoprecipitation experiments with antibodies against the cytoplasmic dynein heavy chain (CDHC) and the nudG CDLC demonstrated that some fraction of the cytoplasmic dynein light chain is in a protein complex with the CDHC. Sucrose gradient sedimentation analysis, however, showed that not all of the NUDG protein is complexed with the heavy chain. A double mutant carrying a cytoplasmic dynein heavy chain deletion plus a temperature-sensitive nudG mutation grew no more slowly at restrictive temperature than a strain with only the CDHC deletion. This result demonstrates that the effect of the nudG mutation on nuclear migration and growth is mediated through an interaction with the CDHC rather than with some other molecule (e.g., myosin-V) with which the 8-kD CDLC might theoretically interact.

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Section: Discussionsupporting

confidence: 89%

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confidence: 91%

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confidence: 99%

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The “8-kD” Cytoplasmic Dynein Light Chain Is Required for Nuclear Migration and for Dynein Heavy Chain Localization in Aspergillus nidulans

Beckwith¹,

Roghi²,

Liu³

et al. 1998

The Journal of Cell Biology

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“…In a healthy organism during the vegetative growth the nuclei migrate towards the growing tip of the hyphae 5 , whereas in mutants with impaired nud genes the nuclei are clustered together following karyokinesis and unable to undergo translocation 2 . The nud family became a focus of intense interest when it was discovered that one of its members, nudF , encoded a close homologue (42% amino acid sequence identity) of the mammalian Lis1 protein, which is mutated in a debilitating developmental genetic syndrome known as the Miller-Dieker lissencephaly 3,7–9 .…”

Section: Introductionmentioning

confidence: 99%

Structural Features and Chaperone Activity of the NudC Protein Family

Zheng

Cierpicki

Burdette

et al. 2011

Journal of Molecular Biology

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The NudC family consists of four conserved proteins with representatives in all eukaryotes. The archetypal nudC gene from Aspergillus nidulans is a member the nud gene family, involved in maintenance of nuclear migration. This family also includes nudF whose human orthologue, Lis1, codes for a protein essential for brain cortex development. Three paralogues of NudC are known in vertebrates, NudC, NudC-like (NudCL) and NudC-like 2 (NudCL2). The fourth distantly related member of the family, CML66, contains a NudC-like domain. The three principal NudC proteins have no catalytic activity, but appear to play as yet poorly defined roles in proliferating and dividing cells. We present crystallographic and NMR studies of the human NudC protein, and discuss the results in the context of structures recently deposited by Structural Genomics centers, i.e. NudCL and mouse NudCL2. All proteins share the same core CS-domain characteristic for proteins acting either as co-chaperones of Hsp90, or as independent small heat shock proteins. However, while NudC and NudCL dimerize via an N-terminally located coiled-coil, the smaller NudCL2 lacks this motif and instead dimerizes as a result of unique domain swapping. We show that NudC and NudCL, but not NudCL2, inhibit aggregation of several target proteins, consistent with an Hsp90-independent heat shock protein function. Importantly, and in contrast to several previous reports, none of the three proteins are able to form binary complexes with Lis1. The availability of structural information will be of help in further studies of cellular functions of the NudC family.

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“…There is abundant evidence that MTs are required for mitosis and for nuclear migration in filamentous fungi (Heath 1995;Morris and Enos 1992;Morris et al 1995;Plamann et al 1994;Suelmann and Fischer 2000b). However, unlike actin, roles for MTs specifically in hyphal growth are less consistent.…”

Section: Introductionmentioning

confidence: 99%

Growth rate of Aspergillus nidulans hyphae is independent of a prominent array of microtubules

Hubbard

Kaminskyj

2007

Mycol Progress

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Roles for the microtubule (MT) cytoskeleton in fungal growth include mitosis and nuclear migration but otherwise are less clearly understood. Confocal microscopy was used to quantify MT abundance and growth rate in hyphae of a haploid Aspergillus nidulans strain containing green fluorescent protein (GFP)-α-tubulin. There was no correlation between growth rate and MT abundance for 112 growing hyphae in an untreated population. However, 109 nongrowing hyphae from the same group had lower average MT abundance. Results for untreated cells were compared with cells treated for 30-120 min with the MT drugs benomyl and taxol, the actin drug latrunculin B, and with solvents used for the drug treatments. Compared with their respective controls, MT abundance was significantly increased by dimethyl sulfoxide (DMSO), significantly reduced by benomyl, and moderately increased by latrunculin, but was unaffected by ethanol. In the same cells, growth rates were significantly increased by ethanol and taxol, significantly reduced by latrunculin, and unaffected by DMSO. Average hyphal growth rate in the first 60 min following 1 μg/ml benomyl treatment was statistically similar to untreated cells, despite the absence of visible MTs after 2 min of treatment. However, growth rate was significantly reduced by 2.5 μg/ml benomyl over the same time period, implying additional effects at the higher concentration. For individual hyphae in each treatment, growth rates varied over short time periods; treatment with 0.1% ethanol substantially increased this variability. Growth rates of taxol-treated hyphae decreased following fluorescence observation, suggesting a possible application to cancer chemotherapy. Overall, there was no correlation between cytoplasmic MT abundance and A. nidulans growth rate within 2 h of cytoskeletal drug or solvent treatment.Abbreviations DIC differential interference contrast GFP green fluorescent protein MT microtubule TEM transmission electron microscopy

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Nuclear migration advances in fungi

Cited by 87 publications

References 37 publications

The “8-kD” Cytoplasmic Dynein Light Chain Is Required for Nuclear Migration and for Dynein Heavy Chain Localization in Aspergillus nidulans

The “8-kD” Cytoplasmic Dynein Light Chain Is Required for Nuclear Migration and for Dynein Heavy Chain Localization in Aspergillus nidulans

Structural Features and Chaperone Activity of the NudC Protein Family

Growth rate of Aspergillus nidulans hyphae is independent of a prominent array of microtubules

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