osk Antibody

1. A missense mutation in the dynactin Arp1 subunit causes most oskar mRNA to localise in the posterior cytoplasm rather than cortically. PMID:29035202
2. oskar transport signals are weak by necessity; their weakness facilitates transfer of the oskar mRNA from the oocyte transport machinery to the machinery for posterior localization. PMID:28760927
3. The long isoform of the protein Oskar regulates the maternal inheritance of mitochondria. Long Oskar traps and maintains mitochondria at the posterior at the site of primordial germ cell (PGC) formation through an actin-dependent mechanism. Mutating long oskar strongly reduces the number of mtDNA molecules inherited by PGCs. Therefore, Long Oskar ensures germline transmission of mitochondria to the next generation. PMID:27923120
4. Crystal structure identifies OSK domain as RNA-binding domain and LOTUS domain as Vasa-binding domain. PMID:26190108
5. Osk has a role in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3'UTRs PMID:26324911
6. The study determined the SOLE structure formed after alternative splicing of Oskar mRNA as an helical structure with few noncanonical base pairs, capped by a pentanucleotide loop that seems could accommodate a protein partner. PMID:26089324
7. results therefore suggest that efficient posterior localization of oskar mRNA requires the concerted activities of both Dynein and Kinesin-1. PMID:24244700
8. These results reveal that Par-1 controls the timing of pole plasm assembly by promoting the localization of oskar mRNA but inhibiting the accumulation of Short Oskar protein. PMID:23948254
9. Oskar protein was required for recruiting EB1 and CLIP-190 to the oocyte posterior; posterior enrichment of EB1 and CLIP-190 is necessary for high levels of endocytosis in this region of the cell; therefore a functional link between dynamic oocyte microtubules and endocytosis. PMID:22561189
10. The study demonstrates that the exon junction complex associates with oskar mRNA upon splicing in vitro and that Drosophila exon junction complex deposition is constitutive and conserved. PMID:22426546
11. report that a Golgi-endosomal protein, Mon2, acts downstream of Osk to remodel cortical actin and to anchor the pole plasm PMID:21610029
12. osk was independently lost in multiple holometabolous insect lineages and that these losses are phylogenetically correlated with changes in germline determination strategies in these species. PMID:21552321
13. Translational repression is mediated by BREs, regulatory elements positioned in two clusters near both ends of the oskar mRNA 3' UTR. PMID:20230756
14. Data indicate that posteriorly localized Par-1 regulates posterior patterning by stabilizing Osk. PMID:11951092
15. Data show that cortical anchoring of the posterior determinant Oskar is a crucial step in pole plasm assembly and restriction, required for proper development of Drosophila melanogaster. PMID:12117819
16. Kinesin restricts pole plasm formation to the posterior by moving oskar mRNA away from microtubule-rich lateral and anterior cortical regions. PMID:12134163
17. MOESIN crosslinks actin and cell membrane in Drosophila oocytes and is required for anchoring of this protein. PMID:12477397
18. Data suggest that Orb-mediated cytoplasmic polyadenylation stimulates oskar translation to achieve the high levels of Oskar protein necessary for posterior patterning and germline differentiation. PMID:12538512
19. We conclude that Bruno plays similar roles in translational regulation of gurken and oskar PMID:12591598
20. Cup is a translational repressor of oskar that is required to assemble the oskar mRNA localization machinery. We propose that Cup coordinates localization with translation. PMID:14691132
21. splicing at the first exon-exon junction of oskar RNA is essential for oskar mRNA localization at the posterior pole PMID:15118729
22. Hrp48 colocalizes with oskar mRNA throughout oogenesis, and interacts with its 5' and 3' regulatory regions, suggesting that it binds directly to oskar mRNA to mediate its posterior transport. PMID:15130488
23. The mechanisms that prevent accumulation of Oskar protein until it can be secured at the posterior pole of the oocyte include regulated degradation or inhibition of translational elongation. PMID:15239960
24. The vlsnull mutant shows that valois+ is required for high levels of Oskar protein to accumulate during oogenesis PMID:15634703
25. link between oskar translation control and localization in oogenesis PMID:16715044
26. oskar RNA acts as a scaffold or regulatory RNA essential for development of the oocyte. PMID:16835436
27. Oskar allows nanos mRNA translation in Drosophila embryos by preventing its deadenylation by Smaug/CCR4. PMID:17050620
28. An oskar-dependent positive feedback loop maintains the polarity of the Drosophila oocyte. PMID:17275299
29. A late phase in accumulation of Osk protein, typically not monitored because of imperviousness of late stage oocytes to antibodies, is crucial for body patterning. PMID:17359300
30. We propose that Oskar maintains its localization at the posterior pole through dual functions in regulating endocytosis and F-actin dynamics. PMID:17419993
31. Osk stimulates endosomal cycling, which in turn promotes F-actin reorganization to anchor the pole plasm components to the oocyte cortex. PMID:18272590
32. By following oskar mRNA particles in living oocytes, study shows that the mRNA is actively transported along microtubules in all directions, with a slight bias toward the posterior. PMID:18775316
33. We observe oskar mRNA to oligomerize as hundreds of copies forming large particles which are necessary for its long range transport and localization. We show the formation of these particles occurs in the nurse cell nucleus in an Hrp48-dependent manner PMID:19597554

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UNIGENE: Dm.7184

KEGG: dme:Dmel_CG10901

STRING: 7227.FBpp0081435