Insight into the function of a unique voltage-sensor protein (TMEM266) and its short form in mouse cerebellum Article Swipe
Takafumi Kawai
,
Hirotaka Narita
,
Kohtarou Konno
,
Sharmin Akter
,
Rizki Tsari Andriani
,
Hirohide Iwasaki
,
Shoji Nishikawa
,
Norihiko Yokoi
,
Yuko Fukata
,
Masaki Fukata
,
Pattama Wiriyasermkul
,
Pornparn Kongpracha
,
Shushi Nagamori
,
Keizo Takao
,
Tsuyoshi Miyakawa
,
Manabu Abe
,
Kenji Sakimura
,
Masahiko Watanabe
,
Atsushi Nakagawa
,
Yasushi Okamura
·
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1042/bcj20220033
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.1042/bcj20220033
Voltage-sensing proteins generally consist of voltage-sensor domains and pore-gate domains, forming the voltage-gated ion channels. However, there are several unconventional voltage-sensor proteins that lack pore-gate domains, conferring them unique voltage-sensing machinery. TMEM266, which is expressed in cerebellum granule cells, is one of the interesting voltage-sensing proteins that has a putative intracellular coiled-coil and a functionally unidentified cytosolic region instead of a pore-gate domain. Here, we approached the molecular function of TMEM266 by performing co-immunoprecipitation experiments. We unexpectedly discovered that TMEM266 proteins natively interact with the novel short form splice variants that only have voltage-sensor domains and putative cytosolic coiled-coil region in cerebellum. The crystal structure of coiled-coil region of TMEM266 suggested that these coiled-coil regions play significant roles in forming homodimers. In vitro expression experiments supported the idea that short form TMEM266 (sTMEM266) or full length TMEM266 (fTMEM266) form homodimers. We also performed proximity labeling mass spectrometry analysis for fTMEM266 and sTMEM266 using Neuro-2A, neuroblastoma cells, and fTMEM266 showed more interacting molecules than sTMEM266, suggesting that the C-terminal cytosolic region in fTMEM266 binds to various targets. Finally, TMEM266-deficient animals showed the moderate abnormality in open-field test. The present study provides clues about the novel voltage-sensing mechanism mediated by TMEM266.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1042/bcj20220033
- OA Status
- hybrid
- Cited By
- 1
- References
- 33
- Related Works
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- OpenAlex ID
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All OpenAlex metadata
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https://openalex.org/W4280501690Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1042/bcj20220033Digital Object Identifier
- Title
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Insight into the function of a unique voltage-sensor protein (TMEM266) and its short form in mouse cerebellumWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2022Year of publication
- Publication date
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2022-05-16Full publication date if available
- Authors
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Takafumi Kawai, Hirotaka Narita, Kohtarou Konno, Sharmin Akter, Rizki Tsari Andriani, Hirohide Iwasaki, Shoji Nishikawa, Norihiko Yokoi, Yuko Fukata, Masaki Fukata, Pattama Wiriyasermkul, Pornparn Kongpracha, Shushi Nagamori, Keizo Takao, Tsuyoshi Miyakawa, Manabu Abe, Kenji Sakimura, Masahiko Watanabe, Atsushi Nakagawa, Yasushi OkamuraList of authors in order
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https://doi.org/10.1042/bcj20220033Publisher landing page
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YesWhether a free full text is available
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hybridOpen access status per OpenAlex
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https://doi.org/10.1042/bcj20220033Direct OA link when available
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Cytosol, Cell biology, Coiled coil, Immunoprecipitation, Biology, Cerebellum, Biophysics, Cytoplasm, Intracellular, Biochemistry, Neuroscience, Gene, EnzymeTop concepts (fields/topics) attached by OpenAlex
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1Total citation count in OpenAlex
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2023: 1Per-year citation counts (last 5 years)
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10Other works algorithmically related by OpenAlex
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