Oral Presentation Instructions
For these giving oral presentations, please bring your own laptop. Facilities will be available for connecting both Macs and PCs.
Chlamy 2018 Abstract Format Instructions
Abstracts should be submitted to email@example.com
Abstract submissions are due by May 26, 2018.
The entire abstract should be written single-spaced using 10-point Arial font with 1-inch margins. The title should be in Bold with Capitalization. The name of all authors and their address should then follow; indicate different addresses using superscript numbers. Underline the name of the person making the presentation and include their (email address) in parentheses at the end of the addresses. Leave a 1-line space between the author/address block and the main text. References may be included as necessary using the following format:
Grossman, A. and King, S.M. The 18th International Chlamydomonas meeting. J Chlamy Biol 1, 1-20 (2018)
The entire abstract must not exceed 29 lines. The abstract should be provided as a Word document.
Please use the following as an example:
A Bioactive Peptide Amidating Enzyme is Required for Ciliogenesis
Dhivya Kumar1, Daniela Strenkert3, Crysten E. Blaby-Haas3, Sabeeha S. Merchant3, Richard E. Mains2, Stephen M. King1,, and Betty A. Eipper1,2
1Molecular Biology and Biophysics and 2Neuroscience Depts, University of Connecticut Health Center, USA, 3Chemistry and Biochemistry Dept, UCLA, USA. (firstname.lastname@example.org)
Dynamic regulation of protein and lipid trafficking is essential for ciliogenesis and normal ciliary function. Differential cargo sorting and targeting of ciliary bound vesicles are thus key events needed to maintain the distinct lipidome and proteome of the cilium. However, the mechanisms governing sorting and trafficking of vesicles from the Golgi to cilia remain unclear. Peptidylglycine alpha-amidating monooxygenase (PAM), a type I integral membrane enzyme, is crucial for a final step in bioactive peptide biosynthesis. Glycine-extended peptide intermediates (e.g. vasopressin-Gly) are converted into biologically active, amidated products in the secretory pathway. In addition to its enzymatic activity, this multifunctional protein has roles in signaling to the nucleus via its cytosol-localized C-terminal tail and in altering the actin cytoskeleton. We recently demonstrated a striking evolutionary correlation between the presence of a PAM gene and cilia, leading us to examine its role in Chlamydomonas. We found that the Chlamydomonas genome encodes active PAM enzyme that localizes to the Golgi and is also tightly bound to the ciliary axonemal superstructure. Importantly, the ciliary localization is conserved in mammalian motile and primary cilia (Kumar et al., 2016). With its enzymatic functions in the secretory pathway lumen and cytosolic roles in interacting with cytoskeletal components, PAM is well poised to coordinate post-Golgi trafficking of ciliary-bound vesicles. We have now generated Chlamydomonas amiRNA knockdown strains that have greatly reduced levels of active PAM. Our preliminary analysis indicates that these strains are incapable of assembling cilia past the transition zone and accumulate starch granules, further suggesting a defect in post-Golgi trafficking. An insertional mutant that makes active PAM lacking most of its C-terminal tail is still capable of building cilia. Thus, our current data support a key conserved role for PAM in ciliogenesis; we are further investigating this possibility using knockdown approaches in planaria and mice.
Kumar, D., Blaby-Haas, C. E., Merchant, S. S., Mains, R. E., King, S. M. and Eipper, B. A. Early eukaryotic origins for cilia-associated bioactive peptide-amidating activity. J Cell Sci 129, 943-956 (2016).