Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins

Thomson, Travis; Liu, Niankun; Arkov, Alexey L.; Lehmann, Ruth; Lasko, Paul

doi:10.1016/j.mod.2008.06.005

Cited by 113 publications

(136 citation statements)

References 59 publications

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“…Oskar protein translation is repressed during transport by the RNA-binding protein Bruno and this repression is released by the binding of activators, such as Orb, once the RNA reaches the posterior pole (7)(8)(9)(10)(11). Oskar organizes germ plasm by recruiting other proteins, such as Vasa, Tudor, and Aubergine (12)(13)(14)(15). An important function of germ plasm is the localization of 50-200 germ plasm-associated RNAs (16,17).…”

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Structure of Drosophila Oskar reveals a novel RNA binding protein

Yang

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Oskar (Osk) protein plays critical roles during Drosophila germ cell development, yet its functions in germ-line formation and body patterning remain poorly understood. This situation contrasts sharply with the vast knowledge about the function and mechanism of osk mRNA localization. Osk is predicted to have an N-terminal LOTUS domain (Osk-N), which has been suggested to bind RNA, and a C-terminal hydrolase-like domain (Osk-C) of unknown function. Here, we report the crystal structures of Osk-N and Osk-C. Osk-N shows a homodimer of winged-helix–fold modules, but without detectable RNA-binding activity. Osk-C has a lipase-fold structure but lacks critical catalytic residues at the putative active site. Surprisingly, we found that Osk-C binds the 3′UTRs of osk and nanos mRNA in vitro. Mutational studies identified a region of Osk-C important for mRNA binding. These results suggest possible functions of Osk in the regulation of stability, regulation of translation, and localization of relevant mRNAs through direct interaction with their 3′UTRs, and provide structural insights into a novel protein–RNA interaction motif involving a hydrolase-related domain.

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Structure of Drosophila Oskar reveals a novel RNA binding protein

Yang

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…For example, polar granules in Drosophila melanogaster are produced in the oocyte and serve to specify the germ-cell lineage in the developing embryo (Leatherman and Jongens 2003;Tadros and Lipshitz 2005;Thomson et al 2008). These granules contain specific maternal transcripts that are translated after fertilization.…”

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Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells

Shah¹,

Nostramo²,

Zhang³

et al. 2014

Genetics

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The cytoplasm of the eukaryotic cell is subdivided into distinct functional domains by the presence of a variety of membrane-bound organelles. The remaining aqueous space may be further partitioned by the regulated assembly of discrete ribonucleoprotein (RNP) complexes that contain particular proteins and messenger RNAs. These RNP granules are conserved structures whose importance is highlighted by studies linking them to human disorders like amyotrophic lateral sclerosis. However, relatively little is known about the diversity, composition, and physiological roles of these cytoplasmic structures. To begin to address these issues, we examined the cytoplasmic granules formed by a key set of signaling molecules, the protein kinases of the budding yeast Saccharomyces cerevisiae. Interestingly, a significant fraction of these proteins, almost 20%, was recruited to cytoplasmic foci specifically as cells entered into the G 0 -like quiescent state, stationary phase. Colocalization studies demonstrated that these foci corresponded to eight different granules, including four that had not been reported previously. All of these granules were found to rapidly disassemble upon the resumption of growth, and the presence of each was correlated with cell viability in the quiescent cultures. Finally, this work also identified new constituents of known RNP granules, including the well-characterized processing body and stress granule. The composition of these latter structures is therefore more varied than previously thought and could be an indicator of additional biological activities being associated with these complexes. Altogether, these observations indicate that quiescent yeast cells contain multiple distinct cytoplasmic granules that may make important contributions to their long-term survival.

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“…Chromatoid bodies share several components with somatic processing bodies, such as RNA decapping enzymes and argonaute proteins (14). Similarly, germinal granules in Drosophila and C. elegans exhibit compositional overlap with somatic processing bodies (15,16), leading to a controversy over whether germinal granules are a modified analog of ubiquitous processing bodies or a germline-specific feature.…”

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Tudor domain containing 7 ( Tdrd7 ) is essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis

Tanaka

Hosokawa

Vagin

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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In the male germline in mammals, chromatoid bodies, a specialized assembly of cytoplasmic ribonucleoprotein (RNP), are structurally evident during meiosis and haploidgenesis, but their developmental origin and regulation remain elusive. The tudor domain containing proteins constitute a conserved class of chromatoid body components. We show that tudor domain containing 7 (Tdrd7), the deficiency of which causes male sterility and age-related cataract (as well as glaucoma), is essential for haploid spermatid development and defines, in concert with Tdrd6, key biogenesis processes of chromatoid bodies. Single and double knockouts of Tdrd7 and Tdrd6 demonstrated that these spermiogenic tudor genes orchestrate developmental programs for ordered remodeling of chromatoid bodies, including the initial establishment, subsequent RNP fusion with ubiquitous processing bodies/GW bodies and later structural maintenance. Tdrd7 suppresses LINE1 retrotransposons independently of piwi-interacting RNA (piRNA) biogenesis wherein Tdrd1 and Tdrd9 operate, indicating that distinct Tdrd pathways act against retrotransposons in the male germline. Tdrd6, in contrast, does not affect retrotransposons but functions at a later stage of spermiogenesis when chromatoid bodies exhibit aggresome-like properties. Our results delineate that chromatoid bodies assemble as an integrated compartment incorporating both germline and ubiquitous features as spermatogenesis proceeds and that the conserved tudor family genes act as master regulators of this unique RNP remodeling, which is genetically linked to the male germline integrity in mammals.germ cells | germinal granules | nuage

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Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins

Cited by 113 publications

References 59 publications

Structure of Drosophila Oskar reveals a novel RNA binding protein

Structure of Drosophila Oskar reveals a novel RNA binding protein

Protein Kinases Are Associated with Multiple, Distinct Cytoplasmic Granules in Quiescent Yeast Cells

Tudor domain containing 7 ( Tdrd7 ) is essential for dynamic ribonucleoprotein (RNP) remodeling of chromatoid bodies during spermatogenesis

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