Membrane-bound receptors, which are crucial for mediating several key developmental signals, are synthesized on endoplasmic reticulum (ER). The functional integrity of ER must therefore be important for the regulation of at least some developmental programs. However, the developmental control of ER function is not well understood. Here, we identify the C. elegans protein FARL-11, an ortholog of the mammalian STRIPAK complex component STRIP1/2 (FAM40A/B), as an ER protein. In the C. elegans embryo, we find that FARL-11 is essential for the cell cycle-dependent morphological changes of ER and for embryonic viability. In the germline, FARL-11 is required for normal ER morphology and for membrane localization of the GLP-1/Notch receptor involved in germline stem cell (GSC) maintenance. Furthermore, we provide evidence that PUF-8, a key translational regulator in the germline, promotes the translation of farl-11 mRNA. These findings reveal that ER form and function in the C. elegans germline are post-transcriptionally regulated and essential for the niche-GSC signaling mediated by GLP-1.
The authors declare no competing or financial interests.
K.P., R.M. and K.S. designed the research; K.P. and K.S. mapped the kp35 allele, performed preliminary phenotypic analysis and 3′ reporter fusion experiments; R.M. determined the FARL-11 expression pattern, and performed the EMSA, Co-IP and the genetic interaction studies; K.S. wrote the manuscript. All authors approved the final version of the manuscript.
Research in the K.S. laboratory is supported by grants from the Indian Council of Agricultural Research through the National Fund Scheme; and by the Department of Biotechnology and the Department of Science and Technology, Ministry of Science and Technology, Government of India.
Supplementary information available online at http://dev.biologists.org/lookup/doi/10.1242/dev.134056.supplemental
- Received December 11, 2015.
- Accepted July 21, 2016.