31:
111:
62:, in which sister chromatids are identically separated at the opposite sides of the spindle forming nuclei (Figure 1). The actomyosin ring follows an orderly sequence of events: identification of the active division site, formation of the ring, constriction of the ring, and disassembly of the ring. It is composed of
74:
proteins are also involved in maintaining the stability of the ring and driving its constriction. Apart from cytokinesis, in which the ring constricts as the cells divide (Figure 2), actomyosin ring constriction has also been found to activate during
162:
form an analogous structure out of FtsZ. These structures are not made out of actomyosin, but serve a similar role in constricting and permitting cytokinesis. In plant cells, there is no actomyosin ring. Instead, a
79:. During this process, actin filaments are degraded, preserving the thickness of the ring. After cytokinesis is complete, one of the two daughter cells inherits a remnant known as the midbody ring.
70:
bundles, thus the term actomyosin. The actomyosin ring operates in contractile motion, although the mechanism on how or what triggers the constriction is still an evolving topic. Other
770:
Alberts, B., A. Johnson, J. Lewis, D. Morgan, M. Raff, K. Roberts, and P. Walter, editors. (2015). Molecular
Biology of the Cell, 6th edition. Garland Science: New York. 1464 pp.
432:
Kucera, Ondrej; Siahaan, Valerie; Janda, Daniel; Dijkstra, Sietske H; Pilatova, Eliska; Zatecka, Eva; Diez, Stefan; Braun, Marcus; Lansky, Zdenek (2021).
86:) during telophase initiates constriction of the actomyosin ring by creating a groove that migrates in an inward motion. Rho-kinases such as
269:
840:
34:
Fig.1. Cell cycle showing the formation of the actomyosin ring during telophase or early cytokinesis stage.
167:
grows centrifugally outwards from the center of the plane of division until it fuses with the existing
131:
704:
316:
234:
95:
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Bi, E.; Maddox, P.; Lew, D. J.; Salmon, E. D.; McMillan, J. N.; Yeh, E.; Pringle, J. R. (1998).
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127:
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336:"Force to divide: Structural and mechanical requirements for actomyosin ring contraction"
110:
806:
782:"Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis"
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Fededa, J. P.; Gerlich, D. W. (2012). "Molecular control of animal cell cytokinesis".
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622:"Orchestrating vesicle transport, ESCRTs and kinase surveillance during abscission"
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51:
17:
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Schwayer, C.; Sikora, M.; Slováková, J.; Kardos, R.; Heisenberg, C. P. (2016).
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205:"Actomyosin Ring Formation and Tension Generation in Eukaryotic Cytokinesis"
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59:
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98:(MLC). This mechanism promotes cell-cell contacts and integrity leading to
815:
400:
573:"Dissecting the roles of ROCK isoforms in stress-induced cell detachment"
139:
691:
303:
286:
155:
143:
588:
252:
Mana-Capelli, Sebastian; McCollum, Dannel (2013). "Actomyosin Ring".
135:
682:
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203:
Cheffings, T. H.; Burroughs, N. J.; Balasubramanian, M. K. (2016).
109:
87:
63:
29:
524:"Centrosome asymmetry and inheritance during animal development"
434:"Anillin propels myosin-independent constriction of actin rings"
151:
147:
138:
is heavily involved in the formation of the fungal AMR. In most
181:
Cytokinesis § Actin-myosin ring assembly and contraction
385:"Embryonic ring closure: Actomyosin rings do the two-step"
90:
has been found to regulate actomyosin contraction through
114:
Fig. 2. The actomyosin ring induces formation of the
724:"Actomyosin ring driven cytokinesis in budding yeast"
130:
then splits by abscission. In fungi, it forms at the
334:Mendes Pinto, I.; Rubinstein, B.; Li, R. (2013).
620:Chen, C. T.; Hehnly, H.; Doxsey, S. J. (2012).
571:Shi, J.; Surma, M.; Zhang, L.; Wei, L. (2013).
287:"Actomyosin networks and tissue morphogenesis"
8:
728:Seminars in Cell & Developmental Biology
54:. It forms perpendicular to the axis of the
82:Activation of the cell-cycle kinase (e.g.
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522:Pelletier, L.; Yamashita, Y. M. (2012).
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118:(4th from top) to assist cell cleavage.
626:Nature Reviews. Molecular Cell Biology
122:In animals, the ring forms along the
27:Cellular formation during cytokinesis
7:
198:
196:
722:Meitinger, F.; Palani, S. (2016).
146:a homologous structure called the
50:, is a prominent structure during
25:
528:Current Opinion in Cell Biology
285:Munjal, A.; Lecuit, T. (2014).
254:Encyclopedia of Systems Biology
1:
262:10.1007/978-1-4419-9863-7_779
740:10.1016/j.semcdb.2016.01.043
500:10.1016/j.devcel.2016.05.024
786:The Journal of Cell Biology
389:The Journal of Cell Biology
857:
450:10.1038/s41467-021-24474-1
106:Variation between kingdoms
540:10.1016/j.ceb.2012.05.005
352:10.1016/j.bpj.2013.06.033
222:10.1016/j.cub.2016.06.071
798:10.1083/jcb.142.5.1301
483:"Actin Rings of Power"
383:Martin, A. C. (2016).
119:
35:
438:Nature Communications
401:10.1083/jcb.201610061
126:on the inside of the
113:
33:
671:Nature Cell Biology
340:Biophysical Journal
58:towards the end of
487:Developmental Cell
304:10.1242/dev.091645
120:
96:myosin light chain
36:
841:Protein complexes
583:(10): 1492–1900.
271:978-1-4419-9862-0
215:(15): R719–R737.
56:spindle apparatus
40:molecular biology
16:(Redirected from
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297:(9): 1789–1793.
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134:before mitosis.
48:contractile ring
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18:Contractile ring
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154:, a homolog of
132:mother-bud neck
128:plasma membrane
124:cleavage furrow
116:cleavage furrow
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92:phosphorylation
44:actomyosin ring
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677:(5): 440–447.
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632:(8): 483–488.
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493:(6): 493–506.
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395:(3): 301–303.
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256:. p. 8.
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150:forms out of
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77:wound closure
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160:Chloroplasts
121:
81:
72:cytoskeletal
47:
43:
37:
692:11336/20338
444:(1): 4595.
291:Development
102:formation.
84:Rho-kinases
52:cytokinesis
830:Categories
577:Cell Cycle
187:References
165:cell plate
734:: 19–27.
169:cell wall
142:and many
68:myosin II
60:telophase
758:26845196
701:22552143
656:22781903
607:23598717
558:22683192
509:27326928
468:34321459
419:27799371
370:23931302
313:24757001
231:27505246
175:See also
140:bacteria
100:adhesion
836:Mitosis
816:9732290
807:2149343
749:4884668
709:3355851
647:4215936
598:3680529
549:3425708
459:8319318
410:5100299
361:3736747
321:5257808
239:3908927
156:tubulin
144:archaea
94:of the
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148:Z-ring
136:Septin
705:S2CID
317:S2CID
235:S2CID
88:ROCK1
64:actin
42:, an
812:PMID
754:PMID
697:PMID
652:PMID
603:PMID
554:PMID
505:PMID
464:PMID
415:PMID
366:PMID
309:PMID
266:ISBN
227:PMID
152:FtsZ
66:and
802:PMC
794:doi
790:142
744:PMC
736:doi
687:hdl
679:doi
642:PMC
634:doi
593:PMC
585:doi
544:PMC
536:doi
495:doi
454:PMC
446:doi
405:PMC
397:doi
393:215
356:PMC
348:doi
344:105
299:doi
295:141
258:doi
217:doi
46:or
38:In
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