Synthetic polyamines: new compounds specific to actin dynamics for mammalian cell and fission yeast.
Résumé
Actin is a major actor in the determination of cell shape. On the one hand, site-directed assembly/disassembly cycles of actin filaments drive protrusive force leading to lamellipodia and filopodia dynamics. Force produced by actin similarly contributes in membrane scission in endocytosis or Golgi remodeling. On the other hand, cellular processes like adhesion, immune synapse, cortex dynamics or cytokinesis are achieved by combining acto-myosin contractility and actin assembly in a complex and not fully understood manner. New chemical compounds are therefore needed to disentangle acto-myosin and actin dynamics. We have found that synthetic, cell permeant, short polyamines are promising new actin regulators in this context. They generate growth and stabilization of lamellipodia within minutes by slowing down the actin assembly/disassembly cycle and facilitating nucleation. We now report that these polyamines also slow down cytokinetic ring closure in fission yeast. This shows that these synthetic compounds are active also in yeasts, and these experiments specifically highlight that actin depolymerization is involved in the ring closure. Thus, synthetic polyamines appear to be potentially powerful agents in a quantitative approach to the role of actin in complex processes in cell biology, developmental biology and potentially cancer research.
Mots clés
ADF
Actin depolymerizing factor
BPA
Branched polyamines
EMM5S
Edinburgh Minimal Media with 5 Supplements
F-actin
Filamentous actin
GFP
Green fluorescent protein
MPA
Macrocyclic polyamines
N-WASP
neuronal Wiskott-Aldrich syndrome protein
ROCK
Rho-associated protein kinase
Rlc1
Regulatory light chain 1
actin cytoskeleton
cytokinetic ring
fission yeast
lamellipodia
mammalian cells
synthetic polyamine