Subunit composition of a DEG/ENaC mechanosensory channel of Caenorhabditis elegans

Chen Yushu; Bharill Shashank; Isacoff Ehud Y.Chalfie Martin

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Subunit composition of a DEG/ENaC mechanosensory channel of Caenorhabditis elegans

机译：Subunit composition of a DEG/ENaC mechanosensory channel of Caenorhabditis elegans

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摘要

Caenorhabditis elegans senses gentle touch in the six touch receptor neurons (TRNs) using a mechanotransduction complex that contains the pore-forming degenerin/epithelial sodium channel (DEG/ENaC) proteins MEC-4 and MEC-10. Past work has suggested these proteins interact with the paraoxonase-like MEC-6 and the cholesterol-binding stomatin-like MEC-2 proteins. Using single molecule optical imaging in Xenopus oocytes, we found that MEC-4 forms homotrimers and MEC-4 and MEC-10 form 4: 4: 10 heterotrimers. MEC-6 and MEC-2 do not associate tightly with these trimers and do not influence trimer stoichiometry, indicating that they are not part of the core channel transduction complex. Consistent with the in vitro data, MEC-10, but not MEC-6, formed puncta in TRN neurites that colocalize with MEC-4 when MEC-4 is overexpressed in the TRNs.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2015年第37期|11690-11695|共6页
作者
Chen Yushu; Bharill Shashank; Isacoff Ehud Y.Chalfie Martin;
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作者单位

Columbia Univ, Dept Biol Sci, New York, NY 10027 USA;

Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
mechanosensory channels; DEG/ENaC proteins; channel stoichiometry;

Subunit composition of a DEG/ENaC mechanosensory channel of Caenorhabditis elegans

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