Cloning and functional expression of a `fast' fungal kinesin

Grummt, Maika; Pistor, Susanne; Lottspeich, Friedrich; Schliwa, Manfred

doi:10.1016/s0014-5793(98)00399-8

Cited by 22 publications

(16 citation statements)

References 23 publications

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“…However, only dynein (92,104) and three kinesin motors, kinesin-1, kinesin-3 (67,108), and kinesin-7 (63), have been shown to be essential for filamentous growth. In animal cells, kinesin-1 (conventional kinesin) and kinesin-3 (Unc104/Kif1A) are prominent organelle transporters (13,51), and these motors are also encoded by filamentous fungi (32,46,66,106,116,119,136,141), whereas they are absent from the yeast Saccharomyces cerevisiae. This suggests that both motors could play a role in long-distance transport in fungal hyphae.…”

Section: Microtubule-dependent Kinesins Support Polarized Hyphal Growthmentioning

confidence: 99%

Hyphal Growth: a Tale of Motors, Lipids, and the Spitzenkörper

2007

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Filamentous fungi are a large and evolutionarily successful group of organisms of enormous ecological importance (27,114). Fungi also have a considerable impact on our economy because they serve as bio-factories for the industrial production of proteins (90,130) and because many fungi are human and plant pathogens that pose a threat to public health and agriculture (1,105,124).The basic unit of a filamentous fungus is the hypha, which usually consists of a chain of elongated cells that expand at the apex of the tip cell (10,41,115). Hyphal tip growth is characterized by the initial establishment of one growth site, which is followed by its continuous maintenance. This growth mode is different from budding in the yeast Saccharomyces cerevisiae.Here a short period of polarized apical growth is followed by extended isotrophic growth, which allows delivery of cell wall material over the entire bud surface and which leads to the almost spherical daughter cell (28,68). In contrast, hyphal growth results in an elongated tip cell, which raises new requirements. Among these is the long-distance transport between the subapical part and the apex of the tip cell. It is thought that microtubule (MT)-based motors, including kinesin-1 and kinesin-3, deliver vesicles and growth supplies over long distances to the hyphal tip (see below). However, in agreement with the described differences between hyphal growth and budding, these motors are not even encoded by the genome of S. cerevisiae.Hyphal growth is accompanied by the secretion of exoenzymes that participate in lysis of the substrate or are involved in the synthesis of the fungal cell wall (3, 42). The cell wall can be considered as an extracellular matrix consisting mainly of a meshwork of polysaccharides and manno-proteins that shelters the cell and resists the internal turgor pressure to maintain the shape of the hypha (112).It is currently thought that growth of fungal hyphae is mediated by cytoskeleton-based polar exocytosis at the hyphal tip and cytoplasmic expansion forces that push the cytoplasm against the flexible apical wall (summarized in reference 7). This model is in part based on the phenotypic similarities between fungal cells and plant cells that grow at their tips, such as pollen tubes or root hairs (36). However, phylogenetic comparison of rRNA or conserved proteins demonstrates that fungi are more closely related to animals (6, 131), and there is evidence for amoeboid motility of fungal cells (50). In this article, I will summarize recent results from different fields of fungal cell biology that are instrumental for understanding hyphal tip growth. This includes research on the Spitzenkör-per, the polarisome, the role of the cytoskeleton in endo-and exocytosis, the cellular function of sterol-rich plasma membrane domains, and the mechanism that generates the force for extension of the hypha. Finally, I will integrate all of these results from different fungal systems in a model for hyphal tip growth, and I will end the review by providing directions for ...

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Section: Microtubule-dependent Kinesins Support Polarized Hyphal Growthmentioning

confidence: 99%

Hyphal Growth: a Tale of Motors, Lipids, and the Spitzenkörper

2007

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“…Light chains are not essential for motor activity (Yang et al, 1990), but they are required for in vivo function (Gindhart et al, 1998;Rahmann et al, 1999). Conventional kinesins isolated from various fungal species (Steinberg and Schliwa, 1995;Lehmler et al, 1997;Steinberg, 1997;Grummt et al, 1998;Wu et al, 1998) share significant sequence homology and a similar domain structure with animal conventional kinesins (Kirchner et al, 1999). However, fungal kinesin purifies without light chains (Steinberg and Schliwa, 1996;Steinberg, 1997;Steinberg et al, 1998), and no conserved light chains are present in the genome of fungi, such as Neurospora crassa and Ustilago maydis (our unpublished data).…”

Section: Introductionmentioning

confidence: 99%

Conventional Kinesin Mediates Microtubule-Microtubule Interactions In Vivo

Straube

Hause

Fink

et al. 2006

MBoC

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Conventional kinesin is a ubiquitous organelle transporter that moves cargo toward the plus-ends of microtubules. In addition, several in vitro studies indicated a role of conventional kinesin in cross-bridging and sliding microtubules, but in vivo evidence for such a role is missing. In this study, we show that conventional kinesin mediates microtubulemicrotubule interactions in the model fungus Ustilago maydis. Live cell imaging and ultrastructural analysis of various mutants in Kin1 revealed that this kinesin-1 motor is required for efficient microtubule bundling and participates in microtubule bending in vivo. High levels of Kin1 led to increased microtubule bending, whereas a rigor-mutation in the motor head suppressed all microtubule motility and promoted strong microtubule bundling, indicating that kinesin can form cross-bridges between microtubules in living cells. This effect required a conserved region in the C terminus of Kin1, which was shown to bind microtubules in vitro. In addition, a fusion protein of yellow fluorescent protein and the Kin1tail localized to microtubule bundles, further supporting the idea that a conserved microtubule binding activity in the tail of conventional kinesins mediates microtubule-microtubule interactions in vivo.

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“…The representative myosin with the highest similarity is the skeletal muscle heavy polypeptide 2 (GB Accession #NP_659210) (Allen and Leinwand, 2002). Interestingly, it also shows significant similarity to NUF1 or SPC110 (yeast spindle poly-body spacer protein, Swiss-prot Accession #P32380) (Mirzayan et al, 1992;Kilmartin et al, 1993), centrosome protein 2 (CEP250/c-Nap1, Swiss-prot Novel structure proteins overexpressed in tumor cells N Sang et al Accession #Q9BV73; GB Accession #NP_009117) (Fry et al, 1998;Mayor et al, 2000Mayor et al, , 2002, centromeric protein E (Accession #Q02224) (Yen et al, 1992;Thrower et al, 1995;Chan et al, 1998), kinesin heavy chain (Synkin, Accession #O43093) (Grummt et al, 1998), and Spo15p (S. pombe sporulating protein, Accession #Q10411) (Ikemoto et al, 2000). A conserved domain search revealed that this region has a coiled-coil (Figure 5a and b).…”

Section: Conserved Motifs and Features Of The Predicted Peptidesmentioning

confidence: 99%

A gene highly expressed in tumor cells encodes novel structure proteins

2004

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We isolated several related but distinct cDNA clones encoding novel structure proteins (NSP) when screening a cDNA library. Analysis revealed that these cDNAs and several similar ESTs in the public databases are derived from a single gene of 17 exons that span a minimum of 227-kb region. This gene is located at chromosome 17p11.2, a region frequently amplified in human gliomas and osteosarcomas, and involved in Birt-Hogg-Dube syndrome, a tumor-prone syndrome. The major coding sequences shared by all isolated transcripts are predicted to encode SMC (structural maintenance of chromosome)/ SbcC ATPase motifs and coiled-coil domains commonly seen in motor or structure proteins. Two 5 0 -end and two 3 0 -end variants (type 5a/b and 3a/b, respectively) were identified, making a total of four possible transcripts. Both 5a and 5b variants were detected in human testis mRNA, but only type 5a was detectable in RNA samples extracted from HeLa cells. The unique carboxyl-terminus of 3b contains a Ca 2 þ -dependent actin-binding domain. Immunohistochemistry studies revealed that NSPs were mostly localized to nuclei. Northern blot analysis demonstrated two major bands and the expression levels are tremendously high in testis while barely detectable in other normal tissues examined. Interestingly, NSP5a3a is highly expressed in some tumor cell lines. These results suggest that NSPs represent a new family of structure proteins with a possible role in nuclear dynamics during cell division, and that NSP5a3a may serve as a tumor marker.

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Cloning and functional expression of a `fast' fungal kinesin

Cited by 22 publications

References 23 publications

Hyphal Growth: a Tale of Motors, Lipids, and the Spitzenkörper

Hyphal Growth: a Tale of Motors, Lipids, and the Spitzenkörper

Conventional Kinesin Mediates Microtubule-Microtubule Interactions In Vivo

A gene highly expressed in tumor cells encodes novel structure proteins

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