. Le bulletin biologique. Biologie ; zoologie ; biologie ; biologie marine. Biologie Cellulaire 209 MM est en II- L'activation]-' ' PIB OTP - Rho rho-^ (active) de l'inhibition de la myosine II i01 RhoODI ?". CIpJ OOP •" &Lt ;)• ^-^ Rho Rho"^ (Inactif) B- de la MLCK ROK POP(inactif) P1,y • •" MLC(""""" 7p ROK (Inactif J POP j MLC (inactif). -&Gt ; Figure 1. (.A/ o} Iransdiiction Schéma signal voie impliqués dans Rho-indiiccd mosin II activation (leftl : RhoGDl bloque l'échange du GTP pour PIB anil Mucks activité RhoGTPase (droite). {B) les activités mobiles (vésicules/fieldjmin en mouvement) et le nombre

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. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. CELL BIOLOGY 209 MM is in II activation L-]-' OTP GDP ' Rho -^- Rho (active) Myosin II inhibition RhoODI i01?". CIpJ_OOP <•«•) Rho ^-^» Rho^ (Inactive) B ROK MLCK- MyoP(Inactive) P1 y •, MLC" •(«'""» _ 7p ROK (Inactive J MyoP j MLC (inactive). -> Figure 1. (.A/ Diagram o} signal Iransdiiction pathway involved in Rho-indiiccd mosin II activation (leftl: RhoGDl blocks the exchange of GTP for GDP anil Mucks RhoGTPase activity (right). {B) The motile activities (moving vesicles/fieldjmin) and the number of sliding actin bundles in control extracts and extracts in the presence of 200 nM RabGDl and 200 nM RhoGDl arc shown. (C) The presence of actin filaments and handles was vcri/icil bv fluorescence microscopy (top row) for control extracts and extracts treated with RahGDI and RhoGDl. The same lieltls Lire shown by AVEC-DIC microscopy photographed j min earlier (bottom row). her of vesicles moving/video field/min (v/f/m; motile activity) at 15-min time intervals after GDI addition. RhoGDl inhibited motile activity by 727r (13 ± 1 v/f/m. n = 3) and filament sliding by 68% (Fig. IB). Pseudo-contractile ring formation was similar to the controls (Fig. 1C). On the other hand. 200 nM RabGDl affected neither motile activity nor filament sliding; the motile activity and number of sliding filament bundles were similar to the controls (Fig. IB). In addition, bundles of actin filaments in pseudo-con- tractile rings were similar to the control extracts (Fig. 1C). These studies showed that blocking Rho proteins with RhoGDl inhibited myosin-II-mediated vesicle transport and filament sliding. We conclude, therefore, that Rho proteins are required for contraction of the contractile ring during cytokinesis. The generation of sliding forces between actin filaments is a well-established activity of bipolar filaments of myosin-II. There- fore the observation that actin filaments self

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• bookauthorlilliefrankrat
• booksubjectbiology
• booksubjectzoology