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Calmodulin binds to Drosophila TRP with an unexpected mode.
Chen, Weidi; Shen, Zeyu; Asteriti, Sabrina; Chen, Zijing; Ye, Fei; Sun, Ziling; Wan, Jun; Montell, Craig; Hardie, Roger C; Liu, Wei; Zhang, Mingjie.
Affiliation
  • Chen W; Shenzhen Key Laboratory for Neuronal Structural Biology, Biomedical Research Institute, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen 518036, China; Greater Bay Biomedical Innocenter, Shenzhen Bay Laboratory, Shenzhen 518055, China.
  • Shen Z; Division of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
  • Asteriti S; Department of Physiology, Development and Neuroscience, Cambridge University, Downing St, Cambridge CB2 3EG, UK; Department of Neurosciences, Biomedicine and Movement Science, University of Verona, Verona, Italy.
  • Chen Z; Department of Molecular, Cellular and Developmental Biology, and the Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106, United States.
  • Ye F; Division of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
  • Sun Z; Shenzhen Key Laboratory for Neuronal Structural Biology, Biomedical Research Institute, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen 518036, China.
  • Wan J; Shenzhen Key Laboratory for Neuronal Structural Biology, Biomedical Research Institute, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen 518036, China; Greater Bay Biomedical Innocenter, Shenzhen Bay Laboratory, Shenzhen 518055, China; Division o
  • Montell C; Department of Molecular, Cellular and Developmental Biology, and the Neuroscience Research Institute, University of California, Santa Barbara, Santa Barbara, CA 93106, United States.
  • Hardie RC; Department of Physiology, Development and Neuroscience, Cambridge University, Downing St, Cambridge CB2 3EG, UK.
  • Liu W; Shenzhen Key Laboratory for Neuronal Structural Biology, Biomedical Research Institute, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen 518036, China. Electronic address: liuwei@sphmc.org.
  • Zhang M; Shenzhen Key Laboratory for Neuronal Structural Biology, Biomedical Research Institute, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen 518036, China; Greater Bay Biomedical Innocenter, Shenzhen Bay Laboratory, Shenzhen 518055, China; Division o
Structure ; 29(4): 330-344.e4, 2021 04 01.
Article in En | MEDLINE | ID: mdl-33326749
ABSTRACT
Drosophila TRP is a calcium-permeable cation channel essential for fly visual signal transduction. During phototransduction, Ca2+ mediates both positive and negative feedback regulation on TRP channel activity, possibly via binding to calmodulin (CaM). However, the molecular mechanism underlying Ca2+ modulated CaM/TRP interaction is poorly understood. Here, we discover an unexpected, Ca2+-dependent binding mode between CaM and TRP. The TRP tail contains two CaM binding sites (CBS1 and CBS2) separated by an ∼70-residue linker. CBS1 binds to the CaM N-lobe and CBS2 recognizes the CaM C-lobe. Structural studies reveal the lobe-specific binding of CaM to CBS1&2. Mutations introduced in both CBS1 and CBS2 eliminated CaM binding in full-length TRP, but surprisingly had no effect on the response to light under physiological conditions, suggesting alternative mechanisms governing Ca2+-mediated feedback on the channel activity. Finally, we discover that TRPC4, the closest mammalian paralog of Drosophila TRP, adopts a similar CaM binding mode.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Calmodulin / Drosophila Proteins / Transient Receptor Potential Channels Limits: Animals / Humans Language: En Journal: Structure Journal subject: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Year: 2021 Type: Article Affiliation country: China
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Calmodulin / Drosophila Proteins / Transient Receptor Potential Channels Limits: Animals / Humans Language: En Journal: Structure Journal subject: BIOLOGIA MOLECULAR / BIOQUIMICA / BIOTECNOLOGIA Year: 2021 Type: Article Affiliation country: China