期刊
DEVELOPMENTAL BIOLOGY
卷 350, 期 2, 页码 370-381出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ydbio.2010.12.005
关键词
Jun N-terminal kinase (JNK); KGB-1; Processing bodies; Oocyte RNP granules; miRNA pathway
资金
- NIH National Center for Research Resources (NCRR)
- MU NIH [5T32GM008396]
- MU Life Sciences
- National Science Foundation NSF [MRI 0923155, IOS 0819713]
- National Institute of Health [1 R15 GM078157-01]
- Div Of Biological Infrastructure
- Direct For Biological Sciences [0923155] Funding Source: National Science Foundation
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 (INK), 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 OCR-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. (C) 2010 Elsevier Inc. All rights reserved.
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