ArticleProceedings of the National Academy of Sciences of the United States of America2007
Drosophila TRP channels require a protein with a distinctive motif encoded by the inaF locus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 18 citations in OpenAlex.
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- Significant contribution of TRPC6 channel-mediated CaJournal of smooth muscle research = Nihon Heikatsukin Gakkai kikanshi · 2016Review
- Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.G3 (Bethesda, Md.) · 2015Article
- PDA (prolonged depolarizing afterpotential)-defective mutants: the story of nina's and ina's--pinta and santa maria, too.Journal of neurogenetics · 2012Review
- The history of the Drosophila TRP channel: the birth of a new channel superfamily.Journal of neurogenetics · 2010Review
- Genetic effects in Drosophila on the potency of diverse general anesthetics: a distinctive pattern of altered sensitivity.Journal of neurogenetics · 2009Article
- Distinct TRP channels are required for warm and cool avoidance in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
In both vertebrates and invertebrates, ion channels of the TRP superfamily are known to be influenced by a variety of accessory factors, but the list of interacting proteins is acknowledged to be incomplete. Although previous work showed that Drosophila TRP function is disrupted by mutations in the inaF locus, the mechanism of this effect has remained obscure. Here we show that a previously overlooked small protein, INAF-B, is encoded by the locus and fulfills its critical role in retinal physiology. The 81-aa INAF-B gene product is an integral membrane protein that colocalizes to rhabdomeres along with TRP channels. Immunoprecipitation experiments demonstrate that the two proteins participate in a complex, and blotting experiments show that neither protein survives in the absence of the other. Both proteins are normally part of a large supramolecular assembly, the signalplex, but their interaction persists even in the absence of the scaffold for this structure. The inaF locus encodes three other proteins, each of which has diverged from INAF-B except for a 32-aa block of residues that encompasses a transmembrane domain. This conserved sequence defines an inaF motif, representatives of which are found in proteins from organisms as diverse as nematodes, fish, and humans. Given the role of INAF-B, these proteins are good candidates for interacting partners of other members of the TRP superfamily.
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