Author: Monika Abedin Sigg; Tabea Menchen; Jeffery Johnson; Chanjae Lee; Semil P. Choksi; Galo Garcia; Henriette Busengdal; Gerard Dougherty; Petra Pennekamp; Claudius Werner; Fabian Rentzsch; Nevan Krogan; John B. Wallingford; Heymut Omran; Jeremy F. Reiter
Title: Evolutionary proteomics uncovers ciliary signaling components Document date: 2017_6_22
ID: 9y8r277c_28
Snippet: Unlike Hh and GPCR signaling proteins, TRP channels and TRP channel-associated 344 protein were detected in all three ciliomes ( Figure 4B ). PKD family members, previously known 345 to localize to cilia, were present in sea anemone and sea urchin cilia, as was TRPM3, a channel 346 that has multiple proposed functions, including heat sensation (Held et al., 2015) . A homolog of 347 TRPM2 was identified in the choanoflagellate cilia, suggesting th.....
Document: Unlike Hh and GPCR signaling proteins, TRP channels and TRP channel-associated 344 protein were detected in all three ciliomes ( Figure 4B ). PKD family members, previously known 345 to localize to cilia, were present in sea anemone and sea urchin cilia, as was TRPM3, a channel 346 that has multiple proposed functions, including heat sensation (Held et al., 2015) . A homolog of 347 TRPM2 was identified in the choanoflagellate cilia, suggesting that the association of TRP 348 channels with cilia arose before the emergence of animals. Also, Enkurin (ENKUR), a TRP 349 channel interacting protein (Sutton et al., 2004) , was detected in the ciliomes of all three 350 organisms and the Enkurin domain-containing protein, ENKD1, was detected in the sea anemone 351 ciliome. ENKUR was originally identified as a TRP channel interactor expressed by sperm 352 (Sutton et al., 2004) . The identification of ENKUR orthologs in choanoflagellate, sea anemone 353 and sea urchin ciliomes suggests a conserved ciliary function. As evolutionary conservation is 354 associated with increased likelihood of affecting fitness and disease (Hirsh and The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/153437 doi: bioRxiv preprint From the analysis of cilia of diverse organisms, we sought to uncover conserved proteins 360 whose functions in ciliary biology had been unappreciated. As mammalian ENKUR has been 361 detected at the sperm flagellum (Sutton et al., 2004) , we wondered if ENKUR had functions in 362 cilia and if those functions were conserved in earlier branching animals. In addition to 363 identifying ENKUR in the ciliomes of choanoflagellates, sea anemones and sea urchins we found 364
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