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Published on: December 31, 2013
Identification and characterization of a Ca2+ -sensitive interaction of the vanilloid receptor TRPV1 with tubulin
C Goswami1, M Dreger, R Jahnel
1Freie Universität Berlin, Institute für Chemie-Biochemie, Berlin, Germany.
Abstract:
The vanilloid receptor TRPV1 plays a well-established functional role in the detection of a range of chemical and thermal noxious stimuli, such as those associated with tissue inflammation and the resulting pain. TRPV1 activation results in membrane depolarization, but may also trigger intracellular Ca2+ -signalling events. In a proteomic screen for proteins associated with the C-terminal sequence of TRPV1, we identified beta-tubulin as a specific TRPV1-interacting protein. We demonstrate that the TRPV1 C-terminal tail is capable of binding tubulin dimers, as well as of binding polymerized microtubules. The interaction is Ca2+ -sensitive, and affects microtubule properties, such as microtubule sensitivity towards low temperatures and nocodazole. Our data thus provide compelling evidence for the interaction of TRPV1 with the cytoskeleton. The Ca2+ -sensitivity of this interaction suggests that the microtubule cytoskeleton at the cell membrane may be a downstream effector of TRPV1 activation.
Insights
The vanilloid receptor TRPV1 interacts with beta-tubulin and microtubules, influencing cytoskeleton dynamics. This calcium-sensitive interaction suggests TRPV1
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- The vanilloid receptor TRPV1 detects noxious stimuli like heat and chemicals, contributing to pain signaling.
- TRPV1 activation leads to membrane depolarization and intracellular calcium (Ca2+) signaling.
- The C-terminal region of TRPV1 is crucial for its function and interactions.
Purpose of the Study:
- To identify proteins interacting with the C-terminal sequence of TRPV1.
- To investigate the functional consequences of TRPV1 interaction with the cytoskeleton.
- To explore the role of Ca2+ in modulating TRPV1-cytoskeleton interactions.
Main Methods:
- Proteomic screening to identify TRPV1-interacting proteins.
- Biochemical assays to confirm binding of TRPV1 C-terminus to tubulin and microtubules.
- Experiments to assess Ca2+ sensitivity and effects on microtubule properties.
Main Results:
- Beta-tubulin was identified as a specific binding partner for TRPV1.
- The TRPV1 C-terminal tail binds to both tubulin dimers and polymerized microtubules.
- This interaction is sensitive to Ca2+ levels and affects microtubule stability and response to agents like nocodazole.
Conclusions:
- TRPV1 directly interacts with the microtubule cytoskeleton.
- The Ca2+-sensitive interaction suggests the cytoskeleton is a downstream effector of TRPV1 activation.
- This finding provides a novel link between ion channel function and cytoskeletal regulation in pain pathways.
