mGluRs (metabotropic glutamate receptors) are G-protein-coupled receptors that modulate synaptic transmission. The eight mammalian mGluRs form three groups based on sequence and functional similarities: group I (1 and 5), group II (2 and 3) and group III (4, 6–8) mGluRs. In the present study, we used a Y2H (yeast two hybrid) screen to identify proteins that interact with the C-terminal intracellular tail of mGluR3. Prominent among the candidate receptor interacting proteins was calmodulin, a Ca2+ sensor known to bind identifiable sequences in group I and III mGluRs. The Y2H method was used to investigate calmodulin binding to mGluRs but failed to confirm the documented interaction with group III mGluRs. Furthermore, subsequent biochemical analysis showed that calmodulin does not interact with group II mGluRs. This illustrates that certain Ca2+-dependent interactions are not recapitulated in yeast. Moreover, it highlights the necessity for supporting biochemical data to substantiate interactions identified with Y2H methods.
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November 2004
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Conference Article|
October 26 2004
Determining calmodulin binding to metabotropic glutamate receptors with distinct protein-interaction methods
K. Lidwell;
K. Lidwell
1Neuroscience Group, University of Southampton, Southampton, U.K.
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J. Dillon;
J. Dillon
1Neuroscience Group, University of Southampton, Southampton, U.K.
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A. Sihota;
A. Sihota
1Neuroscience Group, University of Southampton, Southampton, U.K.
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V. O'Connor;
V. O'Connor
1
1Neuroscience Group, University of Southampton, Southampton, U.K.
1To whom correspondence should be addressed (email V.M.O'Connor@soton.ac.uk).
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B. Pilkington
B. Pilkington
1Neuroscience Group, University of Southampton, Southampton, U.K.
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Publisher: Portland Press Ltd
Received:
July 05 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2004 The Biochemical Society
2004
Biochem Soc Trans (2004) 32 (5): 868–870.
Article history
Received:
July 05 2004
Citation
K. Lidwell, J. Dillon, A. Sihota, V. O'Connor, B. Pilkington; Determining calmodulin binding to metabotropic glutamate receptors with distinct protein-interaction methods. Biochem Soc Trans 1 November 2004; 32 (5): 868–870. doi: https://doi.org/10.1042/BST0320868
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