Mammalian Septins Nomenclature

Macara, Ian G.; Baldarelli, Richard M.; Field, Christine M.; Glotzer, Michael; Hayashi, Yasuhide; Hsu, Shu Chan; Kennedy, Mary B.; Kinoshita, Makoto; Longtine, Mark S.; Low, Claudia; Maltais, Lois J.; McKenzie, Louise; Mitchison, Timothy J.; Nishikawa, Toru; Noda, Makoto; Petty, Elizabeth M.; Peifer, Mark; Pringle, John R.; Robinson, Phillip J.; Roth, Dagmar; Russell, S. E. H.; Stuhlmann, Heidi; Tanaka, Manami; Tanaka, Tomoo; Trimble, William S.; Ware, Jerry; Zeleznik‐Le, Nancy J.; Zieger, Barbara

doi:10.1091/mbc.e02-07-0438

Cited by 120 publications

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“…Sept6, Sept8, Sept10 and Sept11 are mammalian counterparts of Cdc3 (Spn1), based on sequence similarity [5]. However, other animal septins cannot be classified readily as obvious orthologs of particular classes of septin in yeast, based on their primary structure alone [6]. However, all mammalian septin complexes characterized to date contain both Sept6 (or its close paralogs, Sept8, Sept10 and Sept11) and Sept7; in the fly, the orthologs of Sept6 and Sept7 are Sep2 and Pnut, respectively (Table 1) [44].…”

Section: Hetero-oligomeric Multi-septin Complexes In Animal Cellsmentioning

confidence: 99%

“…The genome of Drosophila melanogaster encodes five septins, Caenorhabditis elegans two and Homo sapiens thirteen (Table 1) [4] (for a comprehensive phylogeny, see [5]). In mammals, differential splicing and alternative translation-initiation sites generate an even greater variety of septin isoforms in specific cell types [5,6]. Interestingly, the genomes of aquatic green algae (Chlamydomonas reinhardtii) and marine phytoplankton (Nannochloris spp.)…”

Section: Introductionmentioning

confidence: 99%

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Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

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Septins are a family of conserved proteins that form hetero-oligomeric complexes that assemble into filaments. The filaments can be organized into linear arrays, coils, rings and gauzes. They serve as membrane-associated scaffolds and as barriers to demarcate local compartments, especially for the establishment of the septation site for cytokinesis. Studies in budding and fission yeast have revealed many of the protein-protein interactions that govern the formation of multi-septin complexes. GTP binding and phosphorylation direct the polymerization of filaments that is required for septin-collar assembly in budding yeast, whereas a homolog of anillin instructs timely formation of the ring of septin filaments at the medial cortex in fission yeast. These insights should aid understanding of the organization and function of the diverse septin structures in animal cells.

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Section: Hetero-oligomeric Multi-septin Complexes In Animal Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Some assembly required: yeast septins provide the instruction manual

Versele

Thorner

2005

Trends in Cell Biology

200

199

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“…The septin family of proteins was first recognized in yeast and now appears to be ubiquitous in fungi and animals, although not in plants (Longtine et al, 1996;Field and Kellogg, 1999;Trimble, 1999;Nguyen et al, 2000;Momany et al, 2001;Macara et al, 2002). Typical septins have a variable N-terminal region, a conserved core that includes the elements of a GTP-binding site, and a variable C-terminal region that (in all but a few cases) includes a predicted coiled-coil domain.…”

Section: Introductionmentioning

confidence: 99%

The Role of Cdc42p GTPase-activating Proteins in Assembly of the Septin Ring in Yeast

Caviston

Longtine

Pringle

et al. 2003

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The septins are a conserved family of GTP-binding, filament-forming proteins. In the yeast Saccharomyces cerevisiae, the septins form a ring at the mother-bud neck that appears to function primarily by serving as a scaffold for the recruitment of other proteins to the neck, where they participate in cytokinesis and a variety of other processes. Formation of the septin ring depends on the Rho-type GTPase Cdc42p but appears to be independent of the actin cytoskeleton. In this study, we investigated further the mechanisms of septin-ring formation. Fluorescence-recovery-after-photobleaching (FRAP) experiments indicated that the initial septin structure at the presumptive bud site is labile (exchanges subunits freely) but that it is converted into a stable ring as the bud emerges. Mutants carrying the cdc42 V36G allele or lacking two or all three of the known Cdc42p GTPase-activating proteins (GAPs: Bem3p, Rga1p, and Rga2p) could recruit the septins to the cell cortex but were blocked or delayed in forming a normal septin ring and had accompanying morphogenetic defects. These phenotypes were dramatically enhanced in mutants that were also defective in Cla4p or Gin4p, two protein kinases previously shown to be important for normal septin-ring formation. The Cdc42p GAPs colocalized with the septins both early and late in the cell cycle, and overexpression of the GAPs could suppress the septin-organization and morphogenetic defects of temperature-sensitive septin mutants. Taken together, the data suggest that formation of the mature septin ring is a process that consists of at least two distinguishable steps, recruitment of the septin proteins to the presumptive bud site and their assembly into the stable septin ring. Both steps appear to depend on Cdc42p, whereas the Cdc42p GAPs and the other proteins known to promote normal septin-ring formation appear to function in a partially redundant manner in the assembly step. In addition, because the eventual formation of a normal septin ring in a cdc42 V36G or GAP mutant was invariably accompanied by a switch from an abnormally elongated to a more normal bud morphology distal to the ring, it appears that the septin ring plays a direct role in determining the pattern of bud growth. INTRODUCTIONThe septin family of proteins was first recognized in yeast and now appears to be ubiquitous in fungi and animals, although not in plants (Longtine et al., 1996;Field and Kellogg, 1999;Trimble, 1999;Nguyen et al., 2000;Momany et al., 2001;Macara et al., 2002). Typical septins have a variable N-terminal region, a conserved core that includes the elements of a GTP-binding site, and a variable C-terminal region that (in all but a few cases) includes a predicted coiled-coil domain. In each species examined to date, there are two or more septins that form heterooligomeric complexes to perform their specific functions. Purified septins from yeast, Drosophila, Xenopus, and mammalian cells form filaments of 7-9 nm diameter and of variable length (Field et al., 1996;Frazier et al., 1998;Hsu et al...

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“…In addition, accumulating genetic and cell biological observations on yeast septins indicate that they are also required for localized chitin deposition, bud site selection, cell cycle control, plasma membrane compartmentalization and for regulating some kinases (for a review see Field and Kellogg, 1999;Gladfelter et al, 2001;Faty et al, 2002). As for mammalian cells, 12 septin genes (Sept1-12) have been identified and some septin transcripts undergo complex splicing, showing the presence of numerous members of mammalian septin family proteins (Macara et al, 2002;Kinoshita, 2003). Sept9 was first identified as a fusion partner gene of mixed lineage leukemia in a case of therapy-related acute myeloid leukemia with a t(11;17)(q23;q25) (Osaka et al, 1999;Taki et al, 1999).…”

Section: Introductionmentioning

confidence: 99%