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2016 ; 113
(40
): E5876-E5885
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Molecular organization of cytokinesis nodes and contractile rings by
super-resolution fluorescence microscopy of live fission yeast
#MMPMID27647921
Laplante C
; Huang F
; Tebbs IR
; Bewersdorf J
; Pollard TD
Proc Natl Acad Sci U S A
2016[Oct]; 113
(40
): E5876-E5885
PMID27647921
show ga
Cytokinesis in animals, fungi, and amoebas depends on the constriction of a
contractile ring built from a common set of conserved proteins. Many fundamental
questions remain about how these proteins organize to generate the necessary
tension for cytokinesis. Using quantitative high-speed fluorescence
photoactivation localization microscopy (FPALM), we probed this question in live
fission yeast cells at unprecedented resolution. We show that nodes, protein
assembly precursors to the contractile ring, are discrete structural units with
stoichiometric ratios and distinct distributions of constituent proteins. Anillin
Mid1p, Fes/CIP4 homology-Bin/amphiphysin/Rvs (F-BAR) Cdc15p, IQ motif containing
GTPase-activating protein (IQGAP) Rng2p, and formin Cdc12p form the base of the
node that anchors the ends of myosin II tails to the plasma membrane, with myosin
II heads extending into the cytoplasm. This general node organization persists in
the contractile ring where nodes move bidirectionally during constriction. We
observed the dynamics of the actin network during cytokinesis, starting with the
extension of short actin strands from nodes, which sometimes connected
neighboring nodes. Later in cytokinesis, a broad network of thick bundles
coalesced into a tight ring around the equator of the cell. The actin ring was
?125 nm wide and ?125 nm thick. These observations establish the organization of
the proteins in the functional units of a cytokinetic contractile ring.