Special type of morphological reorganization induced by phorbol ester: reversible partition of cell into motile and stable domains.

Dugina, Vera B.; Svitkina, Tatyana; Vasiliev, J. M.; Gelfand, Israel M.

doi:10.1073/pnas.84.12.4122

Cited by 32 publications

(26 citation statements)

References 7 publications

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“…4) similar to that observed earlier in fibroblasts (1,2). In differentiated cultures, actinoplast-tubuloplast segregation has already commenced and, now, exposure to PMA induces rapid structural modulation of preexisting neurites.…”

supporting

confidence: 68%

“…Typically, tubuloplasts are formed from collapsed lamellar actinoplasts during a process we termed actinoplast-tubuloplast segregation (1). Spectacular enhancement of these transformations can be induced in fibroblasts by the tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA), an agent that activates protein kinase C (PKC) (2). Analysis of PMA-induced segregation suggests that activation of PKC may alter the interrelationships among the actin microfilament, microtubule, and intermediate filament networks (3)(4)(5)(6).…”

mentioning

confidence: 99%

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Reversible structural alterations of undifferentiated and differentiated human neuroblastoma cells induced by phorbol ester.

Tint

Bonder

Feder

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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Morphological alterations in the structure of undifferentiated and morphologically differentiated human neuroblastoma cells induced by phorbol 12-myristate 13-acetate (PMA), an activator ofprotein kinase C, were ex by video microscopy and immunomorphology. In undifferentiated cells, PMA induce the formation of motile actin-rich lamellas and of stable cylindrical processes rich in microtubules. Formation of stable processes resulted either from the collapse oflamellas or the movement of the cell body away from the base of a process. In differentiated cells, PMA induced the rapid extension of small lamelas and subsequent formation of short-lived elongated processes from the lateral edges of neurites. Additionally, growth cones exhibited enhanced modulation in shape after PMA treatment. These reversible reorganizations were similar to the actinoplast-tubuloplast transformations exhibited by PMA-treated fibroblasts. We suggest that actinoplast-tubuloplast reorganizations play essential roles in morphogenesis where stable cytoplasmic extensions are induced by external stimuli. In particular, PMA-induced reorganizations of neural cells in culture may be a model for morphological modulations that occur in nerve tissue.

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supporting

confidence: 68%

mentioning

confidence: 99%

Reversible structural alterations of undifferentiated and differentiated human neuroblastoma cells induced by phorbol ester.

Tint

Bonder

Feder

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

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“…7). When cell models of control (group 1), Colcemid-treated (group 3), or PMA-and Colcemid-treated (group 4) cultures were incubated in the solutions containing ATP, similar alterations were observed in all groups.…”

Section: Resultsmentioning

confidence: 87%

“…In particular, PMA induces a special type of morphological alteration in certain lines of cultured fibroblasts: these cells are reversibly segregated into motile lamella-forming zones and nonmotile long "tail" processes (7). Experimental analysis of this effect gave us reason to suggest that shape changes are due to PMA-induced alterations of interrelationships between the microtubular system and actin cortex.…”

Section: Introductionmentioning

confidence: 99%

Microtubule-dependent effect of phorbol ester on the contractility of cytoskeleton of cultured fibroblasts.

Lyass

Bershadsky

Vasiliev

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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The effect of the tumor promoter phorbol 12-myristate 13-acetate (PMA) upon the contractility of permeabilized cell models (cytoskeletons) of mouse fibroblasts was examined. Contraction was induced by incubation of cell models in a solution containing ATP and was assessed quantitatively by measuring alterations of the area of cell model projection on the substrate. Immunofluorescence microscopy was used to assess alterations ofcytoskeleton morphology in the course of permeabilization and contraction. It was found that contractility of cell models from PMA-treated fibroblasts was considerably diminished as compared with the models from control fibroblasts. ATP induced only local contraction of certain zones of actin cortex in models from PMA-treated fibroblasts; it did not induce general contraction, characteristic of control models. Normal high contractility was characteristic of the models from the cells preincubated with PMA in combination with Colcemid. PMA is a specific activator of protein kinase C, one of the key enzymes of the membrane signal-transduction pathway. It is suggested that protein kinase C regulates contractility of actin cortex and that the pathway of this regulation has a microtubule-dependent stage blocked by Colcemid.The tumor promoter phorbol 12-myristate 13-acetate (PMA), a phorbol ester that is a specific activator of protein kinase C (1), has been reported to induce various types of alterations of morphology, proliferation, and differentiation in cultured cells (2-6). In particular, PMA induces a special type of morphological alteration in certain lines of cultured fibroblasts: these cells are reversibly segregated into motile lamella-forming zones and nonmotile long "tail" processes (7). Experimental analysis of this effect gave us reason to suggest that shape changes are due to PMA-induced alterations of interrelationships between the microtubular system and actin cortex. Danowski and Harris (8,28) have shown that when cultured fibroblasts are spread on an elastic substrate, PMA decreases their ability to wrinkle this substrate; these data suggest that PMA can regulate the contractility of actin cortex.To study further functional alterations of actin cortex in PMA-treated fibroblasts we examined the effect of ATP on permeabilized preparations of cells (also called cell models or cytoskeletons) from differently treated cultured fibroblasts. These "cell models" have their cytoskeletal structures largely exposed to the external environment. When models are incubated with ATP in the appropriate buffer solution they contract; this contraction is probably due to the actinmyosin interactions within their cortices (9-12).We have found that ATP contractility of models of PMAtreated cells was much weaker than that of the models of control cells. This inhibition of contractility was prevented by Colcemid: cytoskeletons of cells treated by PMA after incubation with Colcemid contracted in ATP solution as readily as did the cytoskeletons of controls.These experiments indicate that protein ...

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“…These opposing effects are likely because of the complement of PKC isoforms and/or substrate proteins expressed in a given cell type (17). PMA is thought to exert its effects on migration by changing adhesiveness and/or actin architecture at the leading edge (18,19). PMA also regulates other actin-based motility events such as neurite outgrowth and endosome rocketing (20,21).…”

mentioning

confidence: 99%

Phosphorylation of Coronin 1B by Protein Kinase C Regulates Interaction with Arp2/3 and Cell Motility

Cai

Holoweckyj

Schaller

et al. 2005

Journal of Biological Chemistry

136

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Coronins are a conserved family of WD repeat-containing, actin-binding proteins that regulate cell motility in a variety of model organisms. Our results show that Coronin 1B is a ubiquitously expressed member of the mammalian Coronin gene family that co-localizes with the Arp2/3 complex at the leading edge of fibroblasts, and co-immunoprecipitates with this complex. Pharmacological experiments show that the interaction between Coronin 1B and the Arp2/3 complex is regulated by protein kinase C (PKC) phosphorylation. Coronin 1B is phosphorylated by PKC both in vitro and in vivo. Using tryptic peptide mapping and mutagenesis, we have identified serine 2 (Ser-2) on Coronin 1B as the major residue phosphorylated by PKC in vivo. Rat2 fibroblasts expressing the Coronin 1B S2A mutant show enhanced ruffling in response to phorbol 12-myristate 13-acetate (PMA) and increased speed in single cell tracking assays. Cells expressing the Coronin 1B S2D mutant have attenuated PMA-induced ruffling and slower cell speed. Expression of the S2A mutant partially protects cells from the inhibitory effects of PMA on cell speed, whereas expression of the S2D mutant renders cells hypersensitive to its effects. These data demonstrate that Coronin 1B regulates leading edge dynamics and cell motility in fibroblasts, and that its ability to control motility and interactions with the Arp2/3 complex are regulated by PKC phosphorylation at Ser-2. Furthermore, Coronin 1B phosphorylation is responsible for a significant fraction of the effects of PMA on fibroblast motility.

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Special type of morphological reorganization induced by phorbol ester: reversible partition of cell into motile and stable domains.

Cited by 32 publications

References 7 publications

Reversible structural alterations of undifferentiated and differentiated human neuroblastoma cells induced by phorbol ester.

Reversible structural alterations of undifferentiated and differentiated human neuroblastoma cells induced by phorbol ester.

Microtubule-dependent effect of phorbol ester on the contractility of cytoskeleton of cultured fibroblasts.

Phosphorylation of Coronin 1B by Protein Kinase C Regulates Interaction with Arp2/3 and Cell Motility

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