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Article

Uncovering principles that control septin-septin interactions.

The Journal of biological chemistry - 31 Aug 2012

Kim Moshe S, Froese Carol D, Xie Hong, Trimble William S

Abstract excerpt

Septins comprise a conserved family of GTPases important in cytokinesis. These proteins polymerize into filaments from rod-shaped heteromeric septin complexes. Septins interact with one another at two interfaces (NC and G) that alternate within the complex. Here, we show that small mutations at the N terminus greatly enhance the formation of SEPT2 homopolymers. Taking advantage of this mutation to examine polymer...

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Identifiers

PMID: 22815479
DOI: 10.1074/jbc.M112.387464
PMCID: PMC3436290

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Uncovering principles that control septin-septin interactions.PMID 22815479Read ↗

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Functional insight into the role of Orc6 in septin complex filament formation in Drosophila.Semantic proximity Read ↗

Assays for genetic dissection of septin filament assembly in yeast, from de novo folding through polymerization.Semantic proximity Read ↗

A Key Piece of the Puzzle: The central tetramer of the <i>Saccharomyces cerevisiae</i> septin protofilament and Its Implications for Self-AssemblySemantic proximity Read ↗

Conquering the complex world of human septins: implications for health and disease.Semantic proximity Read ↗

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Higher-order septin assembly is driven by GTP-promoted conformational changes: evidence from unbiased mutational analysis in Saccharomyces cerevisiae.Semantic proximity Read ↗

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