title: C. elegans Dicer interacts with the P-granule component GLH-1 and both regulate germline RNPs.
abstract: P granules, ribonucleoprotein (RNP) complexes specific to the cytoplasmic side of the nuclear pores of Caenorhabditis elegans germ cells, are implicated in post-transcriptional control of maternally-transcribed mRNAs. Here we show a relationship in C. elegans of Dicer, the riboendonuclease processing enzyme of the RNA interference and microRNA pathways, with GLH-1, a germline-specific RNA helicase and a constitutive component of P granules. Based on results from GST-pull-downs and immunoprecipitations, GLH-1 binds DCR-1 and this binding does not require RNA. Both GLH-1 protein and glh-1 mRNA levels are reduced in the dcr-1(ok247) null mutant background; conversely, a reduction of DCR-1 protein is observed in the glh-1(gk100) deletion strain. Thus, in the C. elegans germline, DCR-1 and GLH-1 are interdependent. In addition, evidence indicates that DCR-1 protein levels, like those of GLH-1, are likely regulated by the Jun N-terminal kinase (JNK), KGB-1. In adult germ cells, DCR-1 is found in uniformly-distributed, small puncta both throughout the cytoplasm and the nucleus, on the inner side of nuclear pores, and associated with P granules. In arrested oocytes, GLH-1 and DCR-1 re-localize to cytoplasmic and cortically-distributed RNP granules and are necessary to recruit other components to these complexes. We predict that the GLH-1/DCR-1 complex may function in the transport, deposition, or regulation of maternally-transcribed mRNAs and their associated miRNAs.
authors.affiliation: Molecular Microbiology and Immunology Department, University of Missouri, Columbia, MO 65212, USA.
authors.forename: Erica L
authors.initials: EL
authors.lastname: Beshore
authors.forename: Tamara J
authors.initials: TJ
authors.lastname: McEwen
authors.forename: Molly C
authors.initials: MC
authors.lastname: Jud
authors.forename: Jordan K
authors.initials: JK
authors.lastname: Marshall
authors.forename: Jennifer A
authors.initials: JA
authors.lastname: Schisa
authors.forename: Karen L
authors.initials: KL
authors.lastname: Bennett
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000502:physiology*; D002467:Cell Nucleus / Q000378:metabolism; D053487:DEAD-box RNA Helicases / Q000737:chemistry / Q000502:physiology*; D048031:JNK Mitogen-Activated Protein Kinases / Q000502:physiology; D035683:MicroRNAs / Q000502:physiology; D022022:Nuclear Pore / Q000502:physiology; D009866:Oogenesis; D011485:Protein Binding; D034622:RNA Interference; D016601:RNA-Binding Proteins / Q000502:physiology; D043244:Ribonuclease III / Q000502:physiology*; D012261:Ribonucleoproteins / Q000378:metabolism*
chemical_list: D029742:Caenorhabditis elegans Proteins; D035683:MicroRNAs; C114543:PGL-1 protein, C elegans; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D048031:JNK Mitogen-Activated Protein Kinases; C524496:KGB-1 protein, C elegans; C524497:GLH-1 protein, C elegans; C118116:dcr-1 protein, C elegans; D043244:Ribonuclease III; D053487:DEAD-box RNA Helicases