2016
DOI: 10.1080/15476286.2016.1218592
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The temporally controlled expression of Drongo, the fruit fly homolog of AGFG1, is achieved in female germline cells via P-bodies and its localization requires functional Rab11

Abstract: To achieve proper RNA transport and localization, RNA viruses exploit cellular vesicular trafficking pathways. AGFG1, a host protein essential for HIV-1 and Influenza A replication, has been shown to mediate release of intron-containing viral RNAs from the perinuclear region. It is still unknown what its precise role in this release is, or whether AGFG1 also participates in cytoplasmic transport. We report for the first time the expression patterns during oogenesis for Drongo, the fruit fly homolog of AGFG1. W… Show more

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Cited by 7 publications
(8 citation statements)
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“…A similar redistribution of GalT was induced by the depletion of Garz, consistent with its role in the organization of the secretory pathway in the Drosophila salivary gland (Szul et al, 2011) and with the function of its mammalian ortholog GBF1 at the cis-Golgi (Armbruster and Luschnig, 2012). Interestingly, expressing dsRNA against Arf51F or drongo induced no apparent phenotype regarding the organization of the Golgi (Figures 2A and 2B), consistent with their reported localization at the plasma membrane (Donaldson, 2003;Catrina et al, 2016). These results suggest that Garz, Arf79F, and Arf102F are required for the organization of the Golgi apparatus in border cells.…”
Section: Class I and Class Ii Arfs But Not Drongo Maintain The Integrity Of Golgi Structures In Border Cellssupporting
confidence: 79%
See 1 more Smart Citation
“…A similar redistribution of GalT was induced by the depletion of Garz, consistent with its role in the organization of the secretory pathway in the Drosophila salivary gland (Szul et al, 2011) and with the function of its mammalian ortholog GBF1 at the cis-Golgi (Armbruster and Luschnig, 2012). Interestingly, expressing dsRNA against Arf51F or drongo induced no apparent phenotype regarding the organization of the Golgi (Figures 2A and 2B), consistent with their reported localization at the plasma membrane (Donaldson, 2003;Catrina et al, 2016). These results suggest that Garz, Arf79F, and Arf102F are required for the organization of the Golgi apparatus in border cells.…”
Section: Class I and Class Ii Arfs But Not Drongo Maintain The Integrity Of Golgi Structures In Border Cellssupporting
confidence: 79%
“…We focused on the ArfGAP Drongo, as it seemed to specifically affect the detachment of the border cell cluster at the onset of migration. Drongo is the ortholog of mammalian AGFG1 and was shown to be required for normal egg chamber development (Catrina et al, 2016).…”
Section: Introductionmentioning
confidence: 99%
“…The transcript agfg1 (Arf-GAP domain and FG repeats-containing protein 1) was enriched in low-quality eggs compared with high-quality eggs (1.81 log2FC, FDR = 0.0172) and ahnak (neuroblast differentiation-associated protein ahnak-like) was enriched in low-quality eggs compared with medium-quality eggs (2.01 log2FC, FDR = 0.0026). AGFG1 has been shown to affect the accumulation of a small set of non-polyadenylated cellular mRNAs in mammalian cells [63], and mRNA of Drongo (Drosophila neural GTS1-like), the homolog of AGFG1 in the fruit fly, associates with Me31B (maternal expression of 31B) which is required for the translational repression of maternal mRNAs in the oocyte [64]. AHNAK is considered to be involved in calcium flux regulation and has been proposed to interact with s100 proteins to regulate cellular Ca 2+ homeostasis [65].…”
Section: Resultsmentioning
confidence: 99%
“…To define an optimum number of probes without limiting the f ss-count , we determined the number of probes that have a f ss-count > 0.5 for oskar (osk) mRNA (Fig. 3A), a maternal mRNA that we have successfully visualized in live fruit fly egg chambers using molecular beacons (Bratu et al 2003;Mhlanga et al 2009;Catrina et al 2016). We determined the f ss-count for all osk probes with a probe length ranging between 14 and 28 nt using target structural information from two different PinMol input files, which were obtained with mfold (MFE, 31STR).…”
Section: Defining An Optimum Number Of Selected Probesmentioning
confidence: 99%