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First published online April 1, 2009
doi: 10.1242/10.1242/jcs.034785

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How to scaffold the contractile ring for a safe cytokinesis – lessons from Anillin-related proteins

Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK

View larger version (36K): [in this window] [in a new window]   Fig. 1. Mechanisms and signalling pathways that govern furrow formation and ingression in animal cells. (A) Schematic representation of an animal cell in anaphase and telophase. Chromosomes and nuclei are in grey, microtubules in blue and actomyosin filaments in red. The central spindle, spindle midzone and contractile ring are indicated. (B) RhoA activation at the cleavage site during cytokinesis in Drosophila and vertebrates. Interaction between the RacGAP component of the centralspindlin complex and the RhoGEF Pbl/ECT2 induces the formation of active, GTP-bound RhoA, which in turn promotes (i) profilin-mediated actin polymerization through the family of formin-homologous proteins such as Diaphanous (Dia); and (ii) phosphorylation of the myosin regulatory light chain (MRLC) by two kinases, Rho kinase (ROK) and Citron kinase (CITK). Together, these events promote the sliding of myosin heads along actin filaments, and therefore the formation and ingression of the cleavage furrow.

View larger version (14K): [in this window] [in a new window]   Fig. 2. Secondary structures of Anillin-related proteins in different species. Only ANI-1 and Mid1p are shown for C. elegans and S. pombe, respectively. Characterized and putative domains are shown. Ac, actin-binding domain; AHR, Anillin homology region; Clp1, region necessary for binding to the Cdc14 homologue Clp1/Flp1; Dbox, destruction box; My, myosin-II-binding domain; NES, nuclear export signal; NLS, nuclear localization signal; PH, pleckstrin-homology domain; RacGAP, region that interacts with the RacGAP50C component of the centralspindlin complex; RhoA, region that interacts with the GTPase RhoA; SH3, Src-homology-3-binding consensus sequences. The two putative NLSs nearest the N-terminus in human anillin are situated very close to each other, and are therefore marked by a single symbol.

View larger version (40K): [in this window] [in a new window]   Fig. 3. Localization of Anillin-related proteins during the cell cycle in fission yeast, Drosophila and vertebrates. The distribution of Anillin-related proteins is depicted in red, nuclei in grey, chromosomes in black, and microtubules, centrosomes and spindle-pole bodies in blue. ANI-1 also accumulates at the cleavage furrows in C. elegans embryos, but its distribution in cycling cells has not been described.

View larger version (23K): [in this window] [in a new window]   Fig. 4. A model for Anillin functions in metazoans. Interaction between Anillin and the RacGAP component of the centralspindlin complex connects the actomyosin filaments in the contractile ring with the spindle microtubules. Anillin also functions as a scaffold protein to maximize the efficiency of cleavage furrow ingression by bringing together the signalling and structural components necessary for the assembly and contraction of the actomyosin contractile ring.

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