Abstract
Septins are a family of eukaryotic guanosine phosphate-binding proteins that form linear heterooligomeric complexes, which, in turn, polymerize end-on-end into filaments. These filaments further assemble into higher-order structures at distinct subcellular locations. Dynamic changes in the organization of septin cortex structures appear during cell cycle progression. A variety of regulatory proteins and posttranslational modifications are involved in changes to the structure of septin assemblies during the entire cell cycle. In particular, septin-associated protein kinases mediate changes to septin higher order structures or interconnect cellular morphogenesis with the cell cycle. Yeast cyclin-dependent kinase, a master cell cycle regulator, is required for the initiation of a new septin ring. Here, using epifluoresence and electron microscopy, we show that upon phosphorylation by the Cdc28 kinase, septin filaments disassemble into hetero-octameric building blocks, and that filament depolymerization is specifically G1 cyclin-dependent.
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Abbreviations
- CDK:
-
Cyclin-dependent kinase
- DTT:
-
Dithiothreitol
- EGFP:
-
Enhanced green fluorescent protein
- IPTG:
-
Isopropyl-β-D-thiogalactopyranosid
- NTA:
-
Nitrilotriacetic acid
- PMSF:
-
Phenylmethylsulfonylfluorid
- SD:
-
Standard deviation
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Acknowledgments
We gratefully acknowledge financial support from the Humboldt Foundation 3.4 - 1006989 - SVK - IP (MF and SR) and VEGA (Vedecká Grantová Agentúra, Ministerstvo Školstva Slovenskej Republiky) Grant 2/0002/15 (MF). We thank Jacob Bauer for helpful discussions and critical reading of the manuscript.
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Káčeriková, R., Godočíková, J., Wang, Z. et al. Modulation of septin higher-order structure by the Cdc28 protein kinase. Biologia 73, 1025–1033 (2018). https://doi.org/10.2478/s11756-018-0116-4
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DOI: https://doi.org/10.2478/s11756-018-0116-4