Yu R et al. (2016) Cell "CSR-1 Slices a Balance."

Moazed D, Yu R

[Cell, 2016]

CSR-1 is a germline-expressed C. elegans Argonaute protein essential for viability. In this issue of Cell, Gerson-Gurwitz et al. now demonstrate a role for CSR-1 and its slicer activity in downregulating the levels of maternally deposited mRNAs to fine-tune the expression of proteins with critical roles in embryonic cell divisions.

Worby, Carolyn et al. (2015) International Worm Meeting "Fam20C function in C. elegans."

Desai, Arshad, Dixon, Jack, Oegema, Karen, Worby, Carolyn, Gerson-Gurwitz, Adena

[International Worm Meeting, 2015]

A new family of atypical secreted kinases in human was recently identified, an archetypal member of which is Fam20C. Fam20C phosphorylates S-x-E motifs in caseins and several secreted proteins implicated in bone mineralization. In humans, mutations in Fam20C cause an osteosclerotic bone dysplasia known as Raine syndrome. In addition to biomineralization, phosphorylation by FAM20C is likely to be important for other functions, since many secreted hormones, proteases and other factors have been shown to be phosphorylated on S-x-E motifs.Intriguingly, the C. elegans genome encodes a FAM20C ortholog, which contains a signal-peptide for secretion and phosphorylates proteins within S-x-E motifs in vitro. Since mineralization does not occur in C. elegans, we are hoping to identify new roles for FAM20C in this system.In collaboration with the Oegema and Desai laboratories at UCSD, we are addressing the significance of FAM20C kinase activity in C. elegans. Preliminary work reveals that FAM20C is expressed and localized in the spermatheca and that its deletion leads to germline phenotypes and ~40% embryonic lethality. We are currently investigating potential substrates of FAM20C in C. elegans to determine the molecular basis for the observed phenotypes.