Journal
NATURE
Volume 424, Issue 6949, Pages 685-689Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature01887
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- NICHD NIH HHS [R01 HD037047] Funding Source: Medline
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In many animals, establishment of the germ line depends on segregation of a specialized cytoplasm, or 'germplasm', to a small number of germline precursor cells during early embryogenesis(1). Germ plasm asymmetry involves targeting of RNAs and proteins to a specific region of the oocyte and/or embryo(2). Here we demonstrate that germ plasm asymmetry also depends on degradation of germline proteins in non-germline (somatic) cells. We show that five CCCH finger proteins, components of the Caenorhabditis elegans germ plasm, are targeted for degradation by the novel CCCH-finger-binding protein ZIF-1. ZIF-1 is a SOCS-box protein that interacts with the E3 ubiquitin ligase subunit elongin C. Elongin C, the cullin CUL-2, the ring finger protein RBX-1 and the E2 ubiquitin conjugation enzyme UBC5 (also known as LET-70) are all required in vivo for CCCH finger protein degradation. Degradation is activated in somatic cells by the redundant CCCH finger proteins MEX-5 and MEX-6, which are counteracted in the germ line by the PAR-1 kinase. We propose that segregation of the germ plasm involves both stabilization of germline proteins in the germ line and cullin-dependent degradation in the soma.
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