Distinct pathways control recruitment and maintenance of myosin II at the cleavage furrow during cytokinesis

Dean, Sara; Rogers, Stephen L.; Stuurman, Nico; Vale, Ronald D.; Spudich, James A.

doi:10.1073/pnas.0506810102

Cited by 106 publications

(117 citation statements)

References 47 publications

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“…Myosin II is also known to accumulate at the cleavage furrow and thereby drive cytokinesis. [27][28][29] Immunohistochemical staining also revealed the co-localization of GC UNC-45 with myosin II at the cleavage furrow in mitotic ovarian cancer cells during both metaphase and anaphase ( Figure 5, C and D), consistent with the role of GC UNC-45 as a chaperone that facilitates the correct assembly of myosin II during cytokinesis.…”

Section: Co-localization Of Gc Unc-45 With Myosin II and The Effect Osupporting

confidence: 49%

Myosin II Co-Chaperone General Cell UNC-45 Overexpression Is Associated with Ovarian Cancer, Rapid Proliferation, and Motility

Bazzaro¹,

Santillan²,

Lin

et al. 2007

The American Journal of Pathology

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Both tumor cell proliferation and metastasis are dependent on myosin II. Because UNC-45 is required to chaperone the assembly of a functional myosin II motor, we examined the expression of the general cell (GC) UNC-45 isoform in ovarian tumors. Serous carcinoma expressed elevated levels of GC UNC-45 compared with normal ovarian surface epithelium and benign cystadenoma. High-stage exhibited greater GC UNC-45 expression than low-stage serous carcinoma. Similarly, GC UNC-45 transcripts and protein levels were higher in ovarian cell lines than in immortalized ovarian surface epithelial cells. Elevation of GC UNC-45 levels by ectopic expression enhanced the rate of ovarian cancer cell proliferation, whereas siRNA knockdown of GC UNC-45 suppressed proliferation without altering myosin II levels. GC UNC-45 and myosin II were diffuse within the cytoplasm of confluent interphase cells, but both accumulated together at the cleavage furrow during cytokinesis. GC UNC-45 and myosin II also trafficked to the leading edges of ovarian cancer cells induced to move in a scratch assay. Knockdown of GC UNC-45 reduced the spreading ability of ovarian cancer cells whereas it was enhanced by GC UNC-45 overexpression. In sum, these findings implicate elevated GC UNC-45 protein expression in ovarian carcinoma proliferation and metastasis. Epithelial ovarian cancer is the most lethal gynecological malignancy and the fifth major cause of cancer death among women in the United States. Approximately 70% of ovarian cancer patients are diagnosed with disease that has spread beyond the ovaries when, despite aggressive surgery and chemotherapy, the 5-year survival rate is less than 30%. Ovarian carcinoma rapidly seeds the peritoneal cavity with highly proliferative and invasive cancer cells, and new therapies targeting both of these properties are urgently needed.

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Section: Co-localization Of Gc Unc-45 With Myosin II and The Effect Osupporting

confidence: 49%

Myosin II Co-Chaperone General Cell UNC-45 Overexpression Is Associated with Ovarian Cancer, Rapid Proliferation, and Motility

Bazzaro¹,

Santillan²,

Lin

et al. 2007

The American Journal of Pathology

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“…ZEN-4 is the only kinesin-6 family protein found in Caenorhabditis elegans, and there are two kinesin-6 family proteins found in Drosophila, Pavarotti and KLP67A (Kollmar and Glockner, 2003). Whereas loss of Pavarotti led to a complete failure of cleavage furrow ingression, loss of Zen-4 led to a late cytokinesis defect where the cleavage furrow would initiate but eventually regressed (Adams et al, 1998;Raich et al, 1998;Dean et al, 2005). We have shown that Kif12 null cells have similar cytokinesis defects; some cells fail to initiate cleavage furrow formation (Lakshmikanth et al, 2004), whereas others initiate but fail to complete cytokinesis.…”

Section: Kif12 Is Required For the Localization Of Ddincenp At The CLmentioning

confidence: 60%

The Localization of Inner Centromeric Protein (INCENP) at the Cleavage Furrow Is Dependent on Kif12 and Involves Interactions of the N Terminus of INCENP with the Actin Cytoskeleton

Chen

Lakshmikanth

Spudich

et al. 2007

MBoC

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The inner centromeric protein (INCENP) and other chromosomal passenger proteins are known to localize on the cleavage furrow and to play a role in cytokinesis. However, it is not known how INCENP localizes on the furrow or whether this localization is separable from that at the midbody. Here, we show that the association of Dictyostelium INCENP (DdINCENP) with the cortex of the cleavage furrow involves interactions with the actin cytoskeleton and depends on the presence of the kinesin-6 -related protein Kif12. We found that Kif12 is found on the central spindle and the cleavage furrow during cytokinesis. Kif12 is not required for the redistribution of DdINCENP from centromeres to the central spindle. However, in the absence of Kif12, DdINCENP fails to localize on the cleavage furrow. Domain analysis indicates that the N terminus of DdINCENP is necessary and sufficient for furrow localization and that it binds directly to the actin cytoskeleton. Our data suggest that INCENP moves from the central spindle to the furrow of a dividing cell by a Kif12-dependent pathway. Once INCENP reaches the equatorial cortex, it associates with the actin cytoskeleton where it then concentrates toward the end of cytokinesis.

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“…The contribution of the motor domain of myosin-II proteins to their localization to the cleavage furrow or the contractile ring had previously been unclear because the accumulation of myosin-II to the cleavage furrow or contractile ring was typically concurrent with its filamentogenesis and depended heavily on the tail moiety, but not on the motor domain (Dean et al, 2005). Some scaffold proteins might tether the rod of myosin-II filaments to the equatorial cortex in these cells.…”

Section: Discussion the Motor Properties Of Myo3 Are Relevant To Its mentioning

confidence: 99%

An actin–myosin-II interaction is involved in maintaining the contractile ring in fission yeast

Takaine

Numata

Nakano

2015

Journal of Cell Science

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The actomyosin-based contractile ring, which assembles at the cell equator, maintains its circularity during cytokinesis in many eukaryotic cells, ensuring its efficient constriction. Although consistent maintenance of the ring is one of the mechanisms underpinning cytokinesis, it has not yet been fully addressed. We here investigated the roles of fission yeast myosin-II proteins [Myo2 and Myo3 (also known as Myp2)] in ring maintenance during cytokinesis, with a focus on Myo3. A sitedirected mutational analysis showed that the motor properties of Myo3 were involved in its accumulation in the contractile ring. The assembled ring was often deformed and not properly maintained under conditions in which the activities of myosin-II proteins localizing to the contractile ring were decreased, leading to inefficient cell division. Moreover, Myo3 appeared to form motile clusters on the ring. We propose that large assemblies of myosin-II proteins consolidate the contractile ring by continuously binding to F-actin in the ring, thereby contributing to its maintenance.

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Distinct pathways control recruitment and maintenance of myosin II at the cleavage furrow during cytokinesis

Cited by 106 publications

References 47 publications

Myosin II Co-Chaperone General Cell UNC-45 Overexpression Is Associated with Ovarian Cancer, Rapid Proliferation, and Motility

Myosin II Co-Chaperone General Cell UNC-45 Overexpression Is Associated with Ovarian Cancer, Rapid Proliferation, and Motility

The Localization of Inner Centromeric Protein (INCENP) at the Cleavage Furrow Is Dependent on Kif12 and Involves Interactions of the N Terminus of INCENP with the Actin Cytoskeleton

An actin–myosin-II interaction is involved in maintaining the contractile ring in fission yeast

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