Cytokinesis

Satterwhite, Lisa L.; Pollard, Thomas D.

doi:10.1016/0955-0674(92)90057-j

Cited by 263 publications

(198 citation statements)

References 75 publications

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“…M ANY motile activities of noumuscle cells, including cytokinesis, cell locomotion, and growth cone extension are associated with the reorganization of actin filaments and the formation of new actin-containing structures (Satterwhite and Pollard, 1992;Heath and Holifield, 1991;Mitchison and Kirschner, 1988). At least some of these processes, most notably cell locomotion, have been shown to involve the de novo polymerization of actin filaments (Wang, 1985;Theriot and Mitchison, 1991).…”

mentioning

confidence: 99%

Localization and dynamics of nonfilamentous actin in cultured cells [published erratum appears in J Cell Biol 1993 Nov;123(3):following 767]

Cao¹

1993

The Journal of Cell Biology

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Abstract. Although the distribution of filamentous actin is well characterized in many cell types, the distribution of nonfilamentous actin remains poorly understood. To determine the relative distribution of filamentous and nonfilamentous actin in cultured NRK cells, we have used a number of labeling agents that differ with respect to their specificities toward the filamentous or nonfilamentous form, including monoclonal and polyclonal anti-actin antibodies, vitamin D-binding protein (DBP), and fluorescent phalloidin. Numerous punctate structures were identified that bind poorly to phalloidin but stain positively with several anti-actin antibodies. These bead structures also stain with DBP, suggesting that they are enriched in nonfilamentous actin. Similar punctate structures were observed after the microinjection of fluorescently labeled actin into living cells, allowing us to examine their dynamics in living cells. The actin-containing punctate structures were observed predominantly in the region behind lamellipodia, particularly in spreading cells induced by wounding confluent monolayers. Time-lapse recording of cells injected with fluorescent actin indicated that they form continuously near the leading edge and move centripetally toward the nucleus. Our results suggest that at least part of the unpolymerized actin molecules are localized at discrete sites, possibly as complexes with monomer sequestering proteins. These structures may represent transient storage sites of G-actin within the cell which can be transformed rapidly into actin filaments upon stimulation by specific signals.

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mentioning

confidence: 99%

Localization and dynamics of nonfilamentous actin in cultured cells [published erratum appears in J Cell Biol 1993 Nov;123(3):following 767]

Cao¹

1993

The Journal of Cell Biology

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“…Type II myosins are the best characterized members of the myosin family, essential for muscle contraction and for cytokinesis (Satterwhite and Pollard, 1992;Fishkind and Wang, 1995). All characterized myosin-IIs have heads with similar ATPase mechanisms.…”

Section: Introductionmentioning

confidence: 99%

Myosin-II Tails Confer Unique Functions inSchizosaccharomyces pombe: Characterization of a Novel Myosin-II Tail

Bezanilla

Pollard

2000

MBoC

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Schizosaccharomyces pombe has two myosin-IIs, Myo2p and Myp2p, which both concentrate in the cleavage furrow during cytokinesis. We studied the phenotype of mutant myosin-II strains to examine whether these myosins have overlapping functions in the cell.myo2 + is essential.myp2 + cannot rescue loss ofmyo2 + even at elevated levels of expression.myp2 + is required under specific nutritional conditions; thus myo2 + cannot rescue under these conditions. Studies with chimeras show that the tails rather than the structurally similar heads determine the gene-specific functions ofmyp2 + and myo2 +. The Myo2p tail is a rod-shaped coiled-coil dimer that aggregates in low salt like other myosin-II tails. The Myp2p tail is monomeric in high salt and is insoluble in low salt. Biophysical properties of the full-length Myp2p tail and smaller subdomains indicate that two predicted coiled-coil regions fold back on themselves to form a rod-shaped antiparallel coiled coil. This suggests that Myp2p is the first type II myosin with only one head. The C-terminal two-thirds of Myp2p tail are essential for function in vivo and may interact with components of the salt response pathway.

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“…The function of Myo1p before late anaphase is unknown. In contrast, type II myosin and F-actin in animal cells arrive at the cleavege site at approximately the same time around anaphase (Rappaport, 1996;Satterwhite and Pollard, 1992). Second, the contraction of the actomyosin ring in budding yeast must be coordinated temporally and spatially with septum formation, whereas, in animal cells, a septum does not exist.…”

Section: The Assembly and Function Of The Actomyosin Ring A) Propertimentioning

confidence: 99%

Advances in Cytokinesis Research. Cytokinesis in Budding Yeast: The Relationship between Actomyosin Ring Function and Septum Formation.

2001

Cell Struct. Funct.

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ABSTRACT. Cytokinesis in budding yeast is accomplished by the concerted action of actomyosin ring function and septum formation. The actomyosin ring is not essential for cell viability, but it is required for efficient cell division. Deletion of the actomyosin ring results in abnormal septum formation, and a delay in cytokinesis and cell separation. In contrast, septum formation is essential for cell viability. Block of septum formation prevents the contraction, but not the formation of the actomyosin ring. Here we review and provide additional evidence that defines the functional and molecular relationship between actomyosin ring function and septum formation.

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Cytokinesis

Cited by 263 publications

References 75 publications

Localization and dynamics of nonfilamentous actin in cultured cells [published erratum appears in J Cell Biol 1993 Nov;123(3):following 767]

Localization and dynamics of nonfilamentous actin in cultured cells [published erratum appears in J Cell Biol 1993 Nov;123(3):following 767]

Myosin-II Tails Confer Unique Functions inSchizosaccharomyces pombe: Characterization of a Novel Myosin-II Tail

Advances in Cytokinesis Research. Cytokinesis in Budding Yeast: The Relationship between Actomyosin Ring Function and Septum Formation.

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