Some assembly required: yeast septins provide the instruction manual

Versele, Matthias; Thorner, Jeremy

doi:10.1016/j.tcb.2005.06.007

Cited by 195 publications

(212 citation statements)

References 93 publications

(165 reference statements)

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“…A final aspect of septin function that may be relevant to neoplasia is their formation of complex hetero-oligomeric structures (Versele and Thorner, 2005) and their association with the rho signalling pathway (Nagata and Inagaki, 2005). In yeast, it has been suggested that septins act as scaffolds for the recruitment and regulation of proteins involved in several processes.…”

Section: Other Septins and Cancermentioning

confidence: 99%

“…The 13 known human septins have remarkable similarity, all having in their longest forms (see Figure 1) a central GTP-binding domain flanked by a polybasic region and a so-called septin unique domain (Versele and Thorner, 2005). The function of the GTP-binding domain remains controversial.…”

mentioning

confidence: 99%

“…In particular, the current data are inadequate for the delineation of the potential array of septin hetero-oligomers that might exist. Proteomic and biochemical analyses of specific septins suggest that some specific complexes can form (Versele and Thorner, 2005) and that, for example, SEPT2, 6 and 7 can form a stoichiometric association. In addition, specific coregulation can occur and experimental knock down of one component of this complex by siRNA leads to loss of expression of the other proteins in this complex.…”

mentioning

confidence: 99%

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Do septins have a role in cancer?

Russell

Hall

2005

Br J Cancer

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Septins are an evolutionarily conserved family of genes that encode a P loop-based GTP-binding domain flanked by a polybasic domain and (usually) a coiled-coil region. They have roles in cytokinesis, vesicle trafficking, polarity determination, and can form membrane diffusion barriers, as well as in microtubule and actin dynamics. Septins can form hetero-oligomeric complexes and possibly function as dynamic protein scaffolds. Recently, it has been shown that there are at least 13 human septin genes that exhibit extensive alternate splicing. There are complex patterns of human septin gene expression and recently it has been found that alterations in septin expression are seen in human diseases including neoplasia. This review summarises the essential properties of septins and outlines the accumulating evidence for their involvement in human neoplasia. Septins may belong to the class of cancer critical genes where alteration in expression profile (including alterations in the spectrum of transcripts expressed) may underpin their role in neoplasia as opposed to specific mutational events.

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Section: Other Septins and Cancermentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Do septins have a role in cancer?

Russell

Hall

2005

Br J Cancer

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“…Septins were discovered in the budding yeast Saccharomyces cerevisiae (1) where they organize into a ring at the mother-bud neck during cell division (2). Septins are GTPases of 30 -65 kDa found in most eukaryotes, except plants, sharing an essential role in cytokinesis (3,4).…”

mentioning

confidence: 99%

Septin 11 Restricts InlB-mediated Invasion by Listeria

Mostowy

Danckært

Tham

et al. 2009

Journal of Biological Chemistry

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Septins are filament-forming GTPases implicated in several cellular functions, including cytokinesis. We previously showed that SEPT2, SEPT9, and SEPT11 colocalize with several bacteria entering into mammalian non-phagocytic cells, and SEPT2 was identified as essential for this process. Here, we investigated the function of SEPT11, an interacting partner of SEPT9 whose function is still poorly understood. In uninfected HeLa cells, SEPT11 depletion by siRNA increased cell size but surprisingly did not affect actin filament formation or the colocalization of SEPT9 with actin filaments. SEPT11 depletion increased Listeria invasion, and incubating SEPT11-depleted cells with beads coated with the Listeria surface protein InlB also led to increased entry as compared with control cells. Strikingly, as shown by fluorescence resonance energy transfer, the InlB-mediated stimulation of Met signaling remained intact in SEPT11-depleted cells. Taken together, our results show that SEPT11 is not required for the bacterial entry process and rather restricts its efficacy. Because SEPT2 is essential for the InlB-mediated entry of Listeria, but SEPT11 is not, our findings distinguish the roles of different mammalian septins.Septins were discovered in the budding yeast Saccharomyces cerevisiae (1) where they organize into a ring at the mother-bud neck during cell division (2). Septins are GTPases of 30 -65 kDa found in most eukaryotes, except plants, sharing an essential role in cytokinesis (3, 4). Fourteen septins have been identified in humans and classified on the basis of sequence identity into four distinct groups (3, 5). Septins from different groups polymerize into hetero-oligomeric protein complexes and filaments and may associate with cellular membranes, actin filaments, and microtubules (6, 7). Septins are increasingly regarded as novel cytoskeletal elements (8), but their role in post-mitotic events remains poorly understood.The crystal structure of the SEPT2-SEPT6-SEPT7 complex recently highlighted that septins, as opposed to actin and microtubules, form non-polar filaments (9). In the SEPT7-SEPT6-SEPT2-SEPT2-SEPT6-SEPT7 complex, SEPT2 has a central role in filament formation (9), whereas SEPT6 is thought to be replaceable with other SEPT6 group members, including SEPT11 (3). Widely expressed in mammalian tissues (10), SEPT11 may also be a substitute for SEPT6 in other mammalian septin complexes such as SEPT7-SEPT9-SEPT11 (10) or SEPT5-SEPT7-SEPT11 (11). Because other septins homologous to SEPT11 might compensate for its deficiency (12), the degree to which SEPT11 is required for septin filament structure and function is not yet known. Listeria monocytogenes is an invasive bacterium that enters into most mammalian cells in vitro through the interaction of the bacterial surface protein InlB with its host cellular receptor Met, the hepatocyte growth factor receptor (13). We originally identified SEPT9 associated with phagosomes containing latex beads coated with InlB (14). Given the association of septins with the cytoske...

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“…The yeast bud neck is a special microcompartment, whose structural components and dynamic organization serve as a model for a number of fundamental biological processes related to cytokinesis far beyond yeasts (Versele and Thorner , 2005 ).…”

Section: Cytokinesis and The Yeast Bud Neck Microcompartmentmentioning

confidence: 99%

Microcompartments within the yeast plasma membrane

Merzendorfer

Heinisch

2013

Biological Chemistry

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Recent research in cell biology makes it increasingly clear that the classical concept of compartmentation of eukaryotic cells into different organelles performing distinct functions has to be extended by microcompartmentation, i.e., the dynamic interaction of proteins, sugars, and lipids at a suborganellar level, which contributes significantly to a proper physiology. As different membrane compartments (MCs) have been described in the yeast plasma membrane, such as those defined by Can1 and Pma1 (MCCs and MCPs), Saccharomyces cerevisiae can serve as a model organism, which is amenable to genetic, biochemical, and microscopic studies. In this review, we compare the specialized microcompartment of the yeast bud neck with other plasma membrane substructures, focusing on eisosomes, cell wall integrity-sensing units, and chitin-synthesizing complexes. Together, they ensure a proper cell division at the end of mitosis, an intricately regulated process, which is essential for the survival and proliferation not only of fungal, but of all eukaryotic cells.

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Some assembly required: yeast septins provide the instruction manual

Cited by 195 publications

References 93 publications

Do septins have a role in cancer?

Do septins have a role in cancer?

Septin 11 Restricts InlB-mediated Invasion by Listeria

Microcompartments within the yeast plasma membrane

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