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Forchlorfenuron Alters Mammalian Septin Assembly, Organization, and Dynamics
- Source :
- Journal of Biological Chemistry. 283:29563-29571
- Publication Year :
- 2008
- Publisher :
- Elsevier BV, 2008.
-
Abstract
- Septins are filamentous GTPases that associate with cell membranes and the cytoskeleton and play essential roles in cell division and cellular morphogenesis. Septins are implicated in many human diseases including cancer and neuropathies. Small molecules that reversibly perturb septin organization and function would be valuable tools for dissecting septin functions and could be used for therapeutic treatment of septin-related diseases. Forchlorfenuron (FCF) is a plant cytokinin previously shown to disrupt septin localization in budding yeast. However, it is unknown whether FCF directly targets septins and whether it affects septin organization and functions in mammalian cells. Here, we show that FCF alters septin assembly in vitro without affecting either actin or tubulin polymerization. In live mammalian cells, FCF dampens septin dynamics and induces the assembly of abnormally large septin structures. FCF has a low level of cytotoxicity, and these effects are reversed upon FCF washout. Significantly, FCF treatment induces mitotic and cell migration defects that phenocopy the effects of septin depletion by small interfering RNA. We conclude that FCF is a promising tool to study mammalian septin organization and functions.
- Subjects :
- Small interfering RNA
Pyridines
Cell Cycle Proteins
macromolecular substances
Plasma protein binding
GTPase
Biology
Septin
Models, Biological
Biochemistry
Molecular Basis of Cell and Developmental Biology
Dogs
Cell Movement
GTP-Binding Proteins
Animals
Humans
Cytoskeleton
Molecular Biology
Mitosis
Actin
Wound Healing
Phenylurea Compounds
fungi
Cell migration
Cell Biology
Actins
Phosphoric Monoester Hydrolases
Recombinant Proteins
Cell biology
Cytoskeletal Proteins
Collagen
biological phenomena, cell phenomena, and immunity
Septins
HeLa Cells
Protein Binding
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 283
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....bd4e211cc74405dda4fb5ae4f1b6f11a