Transient posterior localization of a kinesin fusion protein reflects anteroposterior polarity of the Drosophila oocyte

Clark, Ira E.; Giniger, Edward; Ruohola‐Baker, Hannele; Jan, Yuh Nung

doi:10.1016/s0960-9822(00)00068-3

Cited by 280 publications

(250 citation statements)

References 83 publications

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“…It was possible, however, that mutations in the gene were affecting RNA localization by disrupting the microtubule architecture that is a common component of the localization mechanisms of these RNAs (Koch and Spitzer 1983;Stephenson 1991, 1995;Theurkauf et al 1993;for review, see Theurkauf 1994a). In addition, the diffuse osk mRNA pattern that we observed in hls egg chambers has been described in mutants affecting microtubule organization (Ephrussi et al 1991;Kim-Ha et al 1991;Ruohola et al 1991;Clark et al 1994;GonzalezReyes and St. Johnston 1994;Lane and Kalderon 1994;Theurkauf 1994b;Ganzalez-Reyes et al 1995;Roth et al 1995). Hence, we examined the localization of a Kinesin heavy chain:@-Galactosidase (Kin:P-Gal] fusion protein (Clark et al 1994) in a h1s3987 background to analyze one aspect of microtubule structure and function.…”

Section: Microtubule Structure Is Disrupted In Hls Egg Chambersmentioning

confidence: 77%

“…In addition, the diffuse osk mRNA pattern that we observed in hls egg chambers has been described in mutants affecting microtubule organization (Ephrussi et al 1991;Kim-Ha et al 1991;Ruohola et al 1991;Clark et al 1994;GonzalezReyes and St. Johnston 1994;Lane and Kalderon 1994;Theurkauf 1994b;Ganzalez-Reyes et al 1995;Roth et al 1995). Hence, we examined the localization of a Kinesin heavy chain:@-Galactosidase (Kin:P-Gal] fusion protein (Clark et al 1994) in a h1s3987 background to analyze one aspect of microtubule structure and function. In wild-type S8 and S9 egg chambers, microtubule organizing centers (MTOCs) are located at the anterior of the oocyte and direct the formation of a gradient of microtubules whose plus ends extend toward the posterior pole (Theurkauf et al 1992).…”

Section: Microtubule Structure Is Disrupted In Hls Egg Chambersmentioning

confidence: 77%

“…Mutations in these genes result in the mislocalization of several RNAs and proteins, including osk, KIO, and grk mRNAs and Kin:P-Gal and Stau proteins (Ephrussi et al 1991;Kim-Ha et al 1991;St. Johnston et al 1991;Cheung et al 1992;Neuman-Silberberg and Schiipbach 1993;Clark et al 1994). Although these mutants are similar to hls in their variability and range of phenotypes, cytoplasmic streaming initiates normally in hls egg chambers.…”

Section: Hls Contains Homology To Rna-dependent Atpasesmentioning

confidence: 99%

“…For p-Gal staining, ovaries were fixed and stained as described by Clark et al (1994), except that the ovaries were fixed in 0.5% glutaraldehyde. Micrographs were generated on a Nikon Microphot FXA microscope using differential interference contrast optics.…”

Section: Staining and In Situ Hybridization Proceduresmentioning

confidence: 99%

“…Johnston 1993). Both processes, localization of bcd mRNA to the anterior of the oocyte and localization of osk mRNA and Stau protein to the posterior of the oocyte, depend on an organized microtubule network whose orientation is defined by a reciprocal cell-signaling process between germ cells and follicle cells (Pokrywka and Stephenson 1991;Clark et al 1994;Gonzalez-Reyes et al 1995;Roth et al 1995). This signaling cascade requires the activity of Gurken (Grk), a transforming growth factor-a (TGF-a)-like molecule, and Cornichon (Cni), whose precise molecular function is not known, to act in the germ line and signal to the polar follicle cells (Gonzalez-Reyes et al 1995;Roth et al 1995).…”

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confidence: 99%

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Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases.

Gillespie¹,

Berg²

1995

Genes Dev.

154

151

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The homeless (hls) gene of Drosophila is required for anteroposterior and dorsoventral axis formation during oogenesis. At a low frequency, females homozygous for mutations in hls generate early egg chambers in which the oocyte is positioned incorrectly within the cyst. At a high frequency, late-stage egg chambers exhibit a ventralized chorion. Sequence analysis of the hls cDNA predicts a protein with amino-terminal homology to members of the DE-H family of RNA-dependent ATPases and putative helicases. Similarity of 51% in the amino-terminal third of the protein was found to two yeast splicing factors, PRP2 and PRP16, and to Drosophila Maleless, which is required for dosage compensation. To analyze Hls function, RNA localization patterns were determined for seven different transcripts in hls mutant ovaries. Previtellogenic transport to the oocyte was unaffected for all transcripts examined. Transport and localization of bicoid and oskm messages during vitellogenic stages were strongly disrupted, and the distribution and/or quantity of gurken, orb, and fs(3)KIO mRNAs were also affected, but to a lesser degree. In contrast, hu-li tai shao and Biicaudul-D transcripts were transported and localized normally in hls mutants. In addition, Kinesin heavy chain:p-Galactosidase fusion protein failed to localize correctly to the posterior of the oocyte in vitellogenic egg chambers. Examination of the microtubule structure with anti-a-Tubulin antibodies revealed aberrant microtubule organizing center movement and an abnormally dense cytoplasmic microtubule meshwork. We discuss potential roles for Hls in organizing a cytoskeletal framework essential for localizing specific RNAs.

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Section: Microtubule Structure Is Disrupted In Hls Egg Chambersmentioning

confidence: 77%

Section: Microtubule Structure Is Disrupted In Hls Egg Chambersmentioning

confidence: 77%

Section: Hls Contains Homology To Rna-dependent Atpasesmentioning

confidence: 99%

Section: Staining and In Situ Hybridization Proceduresmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases.

Gillespie¹,

Berg²

1995

Genes Dev.

154

151

View full text Add to dashboard Cite

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Poly(A) mRNA is attached to insect ovarian microtubules in vivo in a nucleotide-sensitive manner

Stephen

Talbot

Stebbings

1999

Cell Motil. Cytoskeleton

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Organization and possible functions of microtubule cytoskeleton in hymenopteran nurse cells

Biliński

Jaglarz

1999

Cell Motil. Cytoskeleton

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The results of systematic cytochemical and EM studies on the distribution of actin filaments and microtubules in hymenopteran nurse cells are presented. We demonstrate that each nurse cell nucleus is surrounded by a thick three‐dimensional cage of microtubules that is engaged in maintaining the position of the nuclei in the cell centers during the flow of the cytoplasm from nurse cells into the oocyte. Hence, the cages represent functional counterparts of actin bundles described in the Drosophila nurse cells. Furthermore, our data suggest that a subset of the microtubules is involved in transferring nuage aggregates from the vicinity of the nucleus towards the nurse cell periphery and the nearest intercellular bridge. A conclusion is reached that despite similar polytrophic organization of the ovaries in both hymenopterans and dipterans, the physiology of their nurse cell‐oocyte syncytia appears distinctly different. Cell Motil. Cytoskeleton 43:213–220, 1999. © 1999 Wiley‐Liss, Inc.

show abstract

Transient posterior localization of a kinesin fusion protein reflects anteroposterior polarity of the Drosophila oocyte

Cited by 280 publications

References 83 publications

Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases.

Homeless is required for RNA localization in Drosophila oogenesis and encodes a new member of the DE-H family of RNA-dependent ATPases.

Poly(A) mRNA is attached to insect ovarian microtubules in vivo in a nucleotide-sensitive manner

Organization and possible functions of microtubule cytoskeleton in hymenopteran nurse cells

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