Changes in the state of actin during the exocytotic reaction of permeabilized rat mast cells.

Koffer, Anna; Tatham, Peter E.R.; Gomperts, Bastien D.

doi:10.1083/jcb.111.3.919

Cited by 124 publications

(106 citation statements)

References 43 publications

(51 reference statements)

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“…Immunofluorescence and cytochemical studies demonstrated that F-actin is localized mainly in the cortical region of chromaffin cells (Vitale et al 1991(Vitale et al , 1995 or mast cells (Koffer et al 1990) in the resting state. In the case of cultured normal anterior pituitary cells (Carbajal & Vitale 1997) and pituitaryderived GH4C1 cells (Kiley et al 1992), these cells exhibited bright cortical actin staining, but in GH3B6 cells, the staining was diffuse in the cytoplasm and displayed a patchy aspect at the cell periphery (van de Moortele et al 1991).…”

Section: Discussionmentioning

confidence: 99%

Changes in actin network during calcium-induced exocytosis in permeabilized GH3 cells: calcium directly regulates F-actin disassembly

Yoneda¹,

Nishizaki²,

Tasaka³

et al. 2000

Journal of Endocrinology

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Using digitonin-permeabilized GH3 cells, we investigated both the release of prolactin (PRL) and changes in the cytoskeleton. We determined that permeabilized GH3 cells released PRL in a dose-dependent manner upon addition of micromolar Ca 2+ . Phalloidin, a filamentous actin (F-actin) stabilizing agent, inhibited both Ca 2+ -dependent and -independent PRL release, whereas cytochalasin B, a destabilizing agent, had almost no effect on the release. Observation with a confocal laser scanning microscope revealed that F-actin existed mainly in the cortical region in the quiescent state. Increased cytosolic Ca 2+ induced a change in F-actin distribution: F-actin in the cortical region decreased, whereas F-actin inside the cells increased. This change in F-actin distribution was not observed when phalloidin was added. Addition of cytochalasin B induced patchy F-actin spots, but the pattern of the changes of F-actin distribution did not change. The time course of change in F-actin distribution showed that the F-actin network in the cortical region was reduced within 1 min, and Ca 2+ -dependent release of PRL continued for up to 20 min. These results suggest that the F-actin network near the membrane acts as a barrier to exocytosis and that Ca 2+ directly controls the cytoskeletal changes.

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Section: Discussionmentioning

confidence: 99%

Changes in actin network during calcium-induced exocytosis in permeabilized GH3 cells: calcium directly regulates F-actin disassembly

Yoneda¹,

Nishizaki²,

Tasaka³

et al. 2000

Journal of Endocrinology

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“…FcεRI aggregation triggers cortical F-actin disassembly, which allows access of the secretory vesicles to the plasma membrane (1,8,23,28,34). The process of F-actin disassembly was shown to be dependent on the increase of intracellular Ca 2ϩ (16,23). On the other hand, a powerful regulator of Ca 2ϩ entry and exocytosis in MCs is the serum-and glucocorticoidinducible kinase SGK1 (9,10,33).…”

Section: Mcs and Sgk1mentioning

confidence: 99%

Serum- and glucocorticoid-inducible kinase SGK1 regulates reorganization of actin cytoskeleton in mast cells upon degranulation

Schmid

Yang

et al. 2013

American Journal of Physiology-Cell Physiology

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ϩ/ϩ MCs. When CRAC channels were inhibited by 2-aminoethoxydiphenyl borate (2-APB; 50 M), MC degranulation was strongly decreased in both sgk1 ϩ/ϩ and sgk1 Ϫ/Ϫ MCs and the difference between genotypes was abolished. Moreover, degranulation was impaired by actin-stabilizing (phallacidin) and enhanced by actin-disrupting (cytochalasin B) agents to a similar extent in sgk1 ϩ/ϩ MCs and sgk1Ϫ/Ϫ MCs, implying a regulatory role of actin reorganization in this event. In line with this, measurements of monomeric (G) and filamentous (F) actin content by FACS analysis and Western blotting of detergent-soluble and -insoluble cell fractions indicated an increase of the G/F-actin ratio in sgk1 ϩ/ϩ MCs but not in sgk1MCs upon FcεRI ligation, an observation reflecting actin depolymerization. In sgk1 ϩ/ϩ MCs, FcεRI-induced actin depolymerization was abolished by 2-APB. The observed actin reorganization was confirmed by confocal laser microscopic analysis. Our observations uncover SGK1-dependent Ca 2ϩ entry in mast cells as a novel mechanism regulating actin cytoskeleton. CRAC channel; store-operated Ca 2ϩ entry; 2-APB

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“…No accumulation of F-actin was apparent at the level of cell attachment or at any other plane. Flow cytometric determinations of cellular F-actin content were performed on suspended RP-stained cells as described previously (Koffer et al, 1990).…”

Section: Image Analysismentioning

confidence: 99%

Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins.

Norman

Price

Ridley

et al. 1994

The Journal of Cell Biology

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Abstract. Rat peritoneal mast cells, both intact and permeabilized, have been used widely as model secretory cells. GTP-binding proteins and calcium play a major role in controlling their secretory response. Here we have examined changes in the organization of actin filaments in intact mast cells after activation by compound 48/80, and in permeabilized cells after direct activation of GTP-binding proteins by GTP-'y-S. In both cases, a centripetal redistribution of cellular F-actin was observed: the content of F-actin was reduced in the cortical region and increased in the cell interior. The overall F-actin content was increased.Using permeabilized cells, we show that AIF4-, an activator of heterotrimeric G proteins, induces the disassembly of F-actin at the cortex, while the appearance of actin filaments in the interior of the cell is dependent on two small GTPases, rho and rac. Rho was found to be responsible for de novo actin polymerization, presumably from a membrane-bound monomeric pool, while rac was required for an entrapment of the released cortical filaments. Thus, a heterotrimeric G-protein and the small GTPases, rho and rac, participate in affecting the changes in the actin cytoskeleton observed after activation of mast cells.T HE activation of cell surface receptors leads to a multiplicity of responses, such as movement, secretion, mitosis, or phagocytosis. Most of these are accompanied by changes in the organization of the cytoskeleton. In secretory cells, such cytoskeletal reorganizations have been suggested to play a role in granule migration and in regulating the access of secretory vesicles to the plasma membrane, as well as endocytotic events after exocytosis (Burgoyne and Cheek, 1985;Linstedt and Kelly, 1987;Sontag et al., 1988).Cytoskeletal changes after cell activation have been attributed to changes in pH, Ca 2÷ or phosphorylation (Downey and Grinstein, 1989, Del Castillo et al., 1992, Stossel, 1989Downey et al., 1992) and also to the activation of GTPbinding proteins (Hall, 1992). The latter can work indirectly, via the production of second messengers (such as an increase in Ca2+i, cAME cGMP, or activation of protein kinase C) or via the increased turnover of phosphoinositides, which have been shown to bind to and regulate many actin-binding proteins (Lassing and Lindberg, 1988). However, evidence for direct control of microfilaments by GTPases is accumulating. In electropermeabilized neutrophils, GTP-3~-S was found to induce an increase in F-actin content, even when phospholipase C activity was inhibited (Bengtsson et al., 1990;Therrien and Naccache, 1989 cumulates at cell surface projections directed towards the chemoattractant, has sequence similarities with the/3 subunit of heterotrimeric G-proteins (de Hostos et al., 1991). These/3 subunits have also been found to be associated with the cytoskeleton of mouse lymphoma cells (Carlson et al., 1986). More recently, microinjection studies with cultured fibroblasts showed that two ms-related small GTPases, rho and rac, are essential for the ...

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Changes in the state of actin during the exocytotic reaction of permeabilized rat mast cells.

Cited by 124 publications

References 43 publications

Changes in actin network during calcium-induced exocytosis in permeabilized GH3 cells: calcium directly regulates F-actin disassembly

Changes in actin network during calcium-induced exocytosis in permeabilized GH3 cells: calcium directly regulates F-actin disassembly

Serum- and glucocorticoid-inducible kinase SGK1 regulates reorganization of actin cytoskeleton in mast cells upon degranulation

Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins.

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