{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T17:39:06Z","timestamp":1760204346280},"reference-count":28,"publisher":"The Company of Biologists","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,3,15]]},"abstract":"<jats:p>RIC-3 is a member of a conserved family of proteins that affect nicotinic acetylcholine receptor maturation. In yeast and in vitro, BATH-42, a BTB- and MATH-domain-containing protein, interacts with RIC-3. BATH-42 is also known to interact with the CUL-3 ubiquitin ligase complex. Loss of BATH-42 function leads to increased RIC-3 expression and decreased activity of nicotinic acetylcholine receptors in Caenorhabditis elegans vulva muscles. Increased expression of RIC-3 is deleterious for activity and distribution of nicotinic acetylcholine receptors, and thus the effects of BATH-42 loss of function on RIC-3 expression explain the associated reduction in receptor activity. Overexpression of BATH-42 is also detrimental to nicotinic acetylcholine receptor function, leading to decreased pharyngeal pumping. This effect depends on the C-terminus of RIC-3 and on CUL-3. Thus, our work suggests that BATH-42 targets RIC-3 to degradation via CUL-3-mediated ubiquitylation. This demonstrates the importance of regulation of RIC-3 levels, and identifies a mechanism that protects cells from the deleterious effects of excess RIC-3.<\/jats:p>","DOI":"10.1242\/jcs.036343","type":"journal-article","created":{"date-parts":[[2009,2,18]],"date-time":"2009-02-18T03:13:32Z","timestamp":1234926812000},"page":"807-812","source":"Crossref","is-referenced-by-count":18,"title":["The BTB-MATH protein BATH-42 interacts with RIC-3 to regulate maturation of nicotinic acetylcholine receptors"],"prefix":"10.1242","volume":"122","author":[{"given":"Anna","family":"Shteingauz","sequence":"first","affiliation":[{"name":"Department of Physiology, Hebrew University, Hadassah Medical School, Jerusalem, 91120, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emiliano","family":"Cohen","sequence":"additional","affiliation":[{"name":"Department of Physiology, Hebrew University, Hadassah Medical School, Jerusalem, 91120, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoav","family":"Biala","sequence":"additional","affiliation":[{"name":"Department of Physiology, Hebrew University, Hadassah Medical School, Jerusalem, 91120, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Millet","family":"Treinin","sequence":"additional","affiliation":[{"name":"Department of Physiology, Hebrew University, Hadassah Medical School, Jerusalem, 91120, Israel"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","reference":[{"key":"2021042520483129200_REF1","doi-asserted-by":"crossref","unstructured":"Biala, Y., Liewald, J. 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