The state of the septin cytoskeleton from assembly to function.
Septins are conserved guanine nucleotide-binding proteins that polymerize into filaments at the cell cortex or in association with other cytoskeletal proteins, such as actin or microtubules. As integral players in many morphogenic and signaling events, septins form scaffolds important for the recruitment of the cytokinetic machinery, organization of the plasma membrane, and orientation of cell polarity. Mutations in septins or their misregulation are associated with numerous diseases. Despite growing appreciation for the importance of septins in different aspects of cell biology and disease, septins remain relatively poorly understood compared with other cytoskeletal proteins. Here in this review, we highlight some of the recent developments of the last two years in the field of septin cell biology.
Duke Scholars
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- Septins
- Polymerization
- Multiprotein Complexes
- Microtubules
- Humans
- Fungi
- Eukaryotic Cells
- Developmental Biology
- Cytoskeleton
- Cytoplasm
Citation
Published In
DOI
EISSN
Publication Date
Volume
Start / End Page
Location
Related Subject Headings
- Septins
- Polymerization
- Multiprotein Complexes
- Microtubules
- Humans
- Fungi
- Eukaryotic Cells
- Developmental Biology
- Cytoskeleton
- Cytoplasm