| Literature DB >> 22314400 |
Serge Mostowy1, Pascale Cossart.
Abstract
Septins belong to a family of proteins that is highly conserved in eukaryotes and is increasingly recognized as a novel component of the cytoskeleton. All septins are GTP-binding proteins that form hetero-oligomeric complexes and higher-order structures, including filaments and rings. Recent studies have provided structural information about the different levels of septin organization; however, the crucial structural determinants and factors responsible for septin assembly remain unclear. Investigations on the molecular functions of septins have highlighted their roles as scaffolds for protein recruitment and as diffusion barriers for subcellular compartmentalization in numerous biological processes, including cell division and host-microorganism interactions.Entities:
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Year: 2012 PMID: 22314400 DOI: 10.1038/nrm3284
Source DB: PubMed Journal: Nat Rev Mol Cell Biol ISSN: 1471-0072 Impact factor: 94.444