Systematic analysis of SNARE localization in the filamentous fungus Aspergillus oryzae

Kuratsu, Masahiro; Taura, Ayako; Shoji, Jun‐ya; Kikuchi, Satoko; Arioka, Manabu; Kitamoto, Katsuhiko

doi:10.1016/j.fgb.2007.04.012

Cited by 74 publications

(93 citation statements)

References 76 publications

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“…The localization of SncA homologues has been reported in yeast as well as filamentous fungi, including S. cerevisiae, T. reesei, A. oryzae and A. nidulans (Furuta et al, 2007;Hayakawa et al, 2011;Kuratsu et al, 2007;Taheri-Talesh et al, 2008;Valkonen et al, 2007). Similarly to previous studies in filamentous fungi, GFP-SncA is present in intracellular structures representing secretory vesicles and/or endocytic vesicles.…”

Section: Discussionsupporting

confidence: 60%

“…A possible explanation for this might be the presence of alternative v-SNAREs, which are functionally redundant with SncA. However, all genome annotations of several filamentous fungi, such as T. reesei, Neurospora crassa, A. oryzae, A. nidulans and Aspergillus fumigatus, indicate that these fungi contain only a single copy of sncA in their genome (Gupta & Heath, 2002;Kienle et al, 2009;Kuratsu et al, 2007;Valkonen et al, 2007), as also reported for A. niger (Pel et al, 2007). Still, we considered the possibility of a redundant v-SNARE in the A. niger genome and searched the genome database for a SncA homologue (Table S2).…”

Section: Discussionmentioning

confidence: 99%

“…Compared with S. cerevisiae, An08g07470 is most similar to the vacuolar v-SNARE component Nyv1p, which is involved in homotypic vacuolar docking and fusion (Nichols et al, 1997). In A. oryzae, this v-SNARE is, interestingly, also localized to the plasma membrane, although to a lesser extent than the Snc1p homologue (Kuratsu et al, 2007). Hence, An08g07470 of A. niger could encode a functionally redundant protein for SncA.…”

Section: Discussionmentioning

confidence: 99%

“…Monomeric R-SNARE (v-SNARE) on the vesicle membrane and oligomeric Q-SNAREs on the target membrane form a stable four helix complex called the SNARE complex at each fusion site (Bonifacino & Glick, 2004). The localization of SNARE proteins has been systematically analysed in Aspergillus oryzae and supports the localized distribution of specific SNARE proteins at specific membranes (Kuratsu et al, 2007). In filamentous fungi, the localization of v-SNARE Snc1 and t-SNAREs Sso1 and Sso2 has been studied in detail in T. reesei (Valkonen et al, 2007).…”

Section: Introductionmentioning

confidence: 98%

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Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi

Kwon

Arentshorst

Fiedler³

et al. 2014

Microbiology

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The filamentous fungus Aspergillus niger is an industrially exploited protein expression platform, well known for its capacity to secrete high levels of proteins. To study the process of protein secretion in A. niger, we established a GFP-v-SNARE reporter strain in which the trafficking and dynamics of secretory vesicles can be followed in vivo. The biological role of putative A. niger orthologues of seven secretion-specific genes, known to function in key aspects of the protein secretion machinery in Saccharomyces cerevisiae, was analysed by constructing respective gene deletion mutants in the GFP-v-SNARE reporter strain. Comparison of the deletion phenotype of conserved proteins functioning in the secretory pathway revealed common features but also interesting differences between S. cerevisiae and A. niger. Deletion of the S. cerevisiae Sec2p orthologue in A. niger (SecB), encoding a guanine exchange factor for the GTPase Sec4p (SrgA in A. niger), did not have an obvious phenotype, while SEC2 deletion in S. cerevisiae is lethal. Similarly, deletion of the A. niger orthologue of the S. cerevisiae exocyst subunit Sec3p (SecC) did not result in a lethal phenotype as in S. cerevisiae, although severe growth reduction of A. niger was observed. Deletion of secA, secH and ssoA (encoding SecA, SecH and SsoA the A. niger orthologues of S. cerevisiae Sec1p, Sec8p and Sso1/2p, respectively) showed that these genes are essential for A. niger, similar to the situation in S. cerevisiae. These data demonstrate that the orchestration of exocyst-mediated vesicle transport is only partially conserved in S. cerevisiae and A. niger.

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Section: Discussionsupporting

confidence: 60%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi

Kwon

Arentshorst

Fiedler³

et al. 2014

Microbiology

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“…This functional relationship can also be seen in the filamentous fungus Aspergillus oryzae, where AoVam3p is the sole orthologue of both Sac. cerevisiae Vam3p and Pep12p (Shoji et al, 2006;Kuratsu et al, 2007). Furthermore, although Vsl1p is thought to be the counterpart of Vam7p as we elucidated here, Vsl1p has functional redundancy with Fsv1p.…”

Section: Discussionmentioning

confidence: 63%

Vsl1p cooperates with Fsv1p for vacuolar protein transport and homotypic fusion in Schizosaccharomyces pombe

et al. 2015

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Members of the SNARE protein family participate in the docking-fusion step of several intracellular vesicular transport events. Saccharomyces cerevisiae Vam7p was identified as a SNARE protein that acts in vacuolar protein transport and membrane fusion. However, in Schizosaccharomyces pombe, there have been no reports regarding the counterpart of Vam7p. Here, we found that, although the SPCC594.06c gene has low similarity to Vam7p, the product of SPCC594.06c has a PX domain and SNARE motif like Vam7p, and thus we designated the gene Sch. pombe vsl1 + (Vam7-like protein 1). The vsl1D cells showed no obvious defect in vacuolar protein transport. However, cells of the vsl1D mutant with a deletion of fsv1 + , which encodes another SNARE protein, displayed extreme defects in vacuolar protein transport and vacuolar morphology. Vsl1p was localized to the vacuolar membrane and prevacuolar compartment, and its PX domain was essential for proper localization. Expression of the fusion protein GFP-Vsl1p was able to suppress ZnCl 2 sensitivity and the vacuolar protein sorting defect in the fsv1D cells. Moreover, GFP-Vsl1p was mislocalized in a pep12D mutant and in cells overexpressing fsv1 + . Importantly, overexpression of Sac. cerevisiae VAM7 could suppress the sensitivity to ZnCl 2 of vsl1D cells and the vacuolar morphology defect of vsl1Dfsv1D cells in Sch. pombe. Taken together, these data suggest that Vsl1p and Fsv1p are required for vacuolar protein transport and membrane fusion, and they function cooperatively with Pep12p in the same membrane-trafficking step.

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2012

Fungi and Lignocellulosic Biomass

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Systematic analysis of SNARE localization in the filamentous fungus Aspergillus oryzae

Cited by 74 publications

References 76 publications

Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi

Molecular genetic analysis of vesicular transport in Aspergillus niger reveals partial conservation of the molecular mechanism of exocytosis in fungi

Vsl1p cooperates with Fsv1p for vacuolar protein transport and homotypic fusion in Schizosaccharomyces pombe

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