A protein kinase similar to MAP kinase activator acts downstream of the raf kinase in Drosophila

Tsuda, Leo; Inoué, Yoshihiro; Yoo, Mi‐Ae; Mizuno, Masami; Hata, Mami; Lim, Young-Mi; Adachi‐Yamada, Takashi; Ryo, Haruko; Masamune, Yukito; Nishida, Yasuyoshi

doi:10.1016/0092-8674(93)90117-9

Cited by 212 publications

(94 citation statements)

References 40 publications

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“…Mutant flies used in this study were GMR-p35 (Hay et al, 1994), GMR-diap1 (Hay et al, 1995), GMRdiap2 (Hay et al, 1995), rl Su23 (Lim et al, 1997), Dsor1 Su1 (Tsuda et al, 1993), Df(3L)H99 (White et al, 1994), and GMR-hid (Grether et al, 1995). The HS-Ras1 V12 transgenic strain is a gift from N. Perrimon.…”

Section: Drosophila Stocks and Culturementioning

confidence: 99%

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Argos induces programmed cell death in the developing Drosophila eye by inhibition of the Ras pathway

et al. 1998

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We studied the role of Ras signaling in the regulation of cell death during Drosophila eye development. Overexpression of Argos, a diffusible inhibitor of the EGF receptor and Ras signaling, caused excessive cell death in developing eyes at pupal stages. The Argos-induced cell death was suppressed by coexpression of the anti-apoptotic genes p35, diap1, or diap2 in the eye as well as by the Df(3L)H99 chromosomal deletion that lacks three apoptosis-inducing genes, reaper, head involution defective (hid) and grim. Transient misexpression of the activated Ras1 protein (Ras1 V12 ) later in pupal development suppressed the Argos-induced cell death. Thus, Argos-induced cell death seemed to have resulted from the suppression of the anti-apoptotic function of Ras. Conversely, cell death induced by overexpression of Hid was suppressed by gain-of-function mutations of the genes coding for MEK and ERK. These results support the idea that Ras signaling functions in two distinct processes during eye development, first triggering the recruitment of cells and later negatively regulating cell death.

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Section: Drosophila Stocks and Culturementioning

confidence: 99%

“…Su1 (Tsuda et al, 1993) and rl Su23 , gain-of-function mutations of the genes encoding MEK and ERK, respectively. The external morphology of the Dsor1 Su1 eye is indistinguishable from wildtype (Lim et al, 1997), while the rl Su23 flies have roughened but .…”

Section: Dsor1 and Rolled Function To Prevent Pcd Induced By Hidmentioning

confidence: 99%

Argos induces programmed cell death in the developing Drosophila eye by inhibition of the Ras pathway

et al. 1998

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“…In addition, it has been reported that the promoter of the Drosophila ras2 gene also contains the DRE-like sequence (Lightfoot et al 1994), suggesting that this is another candidate DREF-target gene. Moreover, we searched the Drosophila genome project database for DRE-like sequences and found them in the promoter region of the Dsor1 gene, a Drosophila homologue of mammalian MEK (Tsuda et al 1993). This suggests that the Dsor1 gene can also be a target of DREF.…”

Section: Genes To Cells (2001) 6 877±886mentioning

confidence: 99%

Over‐expression of DREF in the Drosophila wing imaginal disc induces apoptosis and a notching wing phenotype

et al. 2001

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Background: DNA replication-related element binding factor (DREF) has been suggested to be involved in regulation of DNA replication-and proliferationrelated genes in Drosophila. While the effects on the mutation in the DNA replication-related element (DRE) in cultured cells have been studied extensively, the consequences of elevating wild-type DREF activity in developing tissues have hitherto remained unclear.

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“…Our experiments reported here using mutants, specific antibodies to the cross-links, and drugs that affect actin assembly and/or phosphorylation help us understand more about the control of bundle formation in vivo. Once we know what happens in a cell, we can begin to dissect how individual components are regulated, a regulation that ultimately involves cascades orchestrated by cdc42 (Eaton et al 1996) and Ras (Harden et al 1995; Eaton et al 1996), Rho (Strutt et al 1997; Hacker and Perrimon 1998), Raf (Tsuda et al 1993), and Ral (Sawamoto et al 1999). In addition, our results give us clues as to what regulates other features of the actin bundles, such as their shape.…”

Section: Introductionmentioning

confidence: 99%

Regulation of Actin Filament Cross-linking and Bundle Shape in Drosophila Bristles

Tilney

Connelly

Vranich

et al. 2000

The Journal of Cell Biology

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Previous studies demonstrate that in developing Drosophila bristles, two cross-linking proteins are required sequentially to bundle the actin filaments that support elongating bristle cells. The forked protein initiates the process and facilitates subsequent cross-linking by fascin. Using cross-linker–specific antibodies, mutants, and drugs we show that fascin and actin are present in excessive amounts throughout bundle elongation. In contrast, the forked cross-linker is limited throughout bundle formation, and accordingly, regulates bundle size and shape. We also show that regulation of cross-linking by phosphorylation can affect bundle size. Specifically, inhibition of phosphorylation by staurosporine results in a failure to form large bundles if added during bundle formation, and leads to a loss of cross-linking by fascin if added after the bundles form. Interestingly, inhibition of dephosphorylation by okadaic acid results in the separation of the actin bundles from the plasma membrane. We further show by thin section electron microscopy analysis of mutant and wild-type bristles that the amount of material that connects the actin bundles to the plasma membrane is also limited throughout bristle elongation. Therefore, overall bundle shape is determined by the number of actin filaments assembled onto the limited area provided by the connector material. We conclude that assembly of actin bundles in Drosophila bristles is controlled in part by the controlled availability of a single cross-linking protein, forked, and in part by controlled phosphorylation of cross-links and membrane actin connector proteins.

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A protein kinase similar to MAP kinase activator acts downstream of the raf kinase in Drosophila

Cited by 212 publications

References 40 publications

Argos induces programmed cell death in the developing Drosophila eye by inhibition of the Ras pathway

Argos induces programmed cell death in the developing Drosophila eye by inhibition of the Ras pathway

Over‐expression of DREF in the Drosophila wing imaginal disc induces apoptosis and a notching wing phenotype

Regulation of Actin Filament Cross-linking and Bundle Shape in Drosophila Bristles

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