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All three members of the\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    family (\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    1\u20103) have large ecto\u2010domains that form homophilic interactions and encompass more than 2000 amino acids. Mutations in the ecto\u2010domain or other gene locations of\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    s are associated with neural tube defects and other diseases in humans.\n                    <jats:italic>Celsr<\/jats:italic>\n                    knockout (\n                    <jats:styled-content style=\"fixed-case\">KO<\/jats:styled-content>\n                    ) animals have many developmental defects. Therefore, specific agonists or antagonists of\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    members may have therapeutic potential. Although significant progress has been made regarding the functions and biochemical properties of\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    s, our knowledge of these receptors is still lacking, especially considering that they are broadly distributed but have few characterized functions in a limited number of tissues. The dynamic activation and inactivation of\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    s and the presence of endogenous ligands beyond homophilic interactions remain elusive, as do the regulatory mechanisms and downstream signaling of these receptors. Given this motivation, future studies with more advanced cell biology or biochemical tools, such as conditional\n                    <jats:styled-content style=\"fixed-case\">KO<\/jats:styled-content>\n                    mice, may provide further insights into the mechanisms underlying\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    function, laying the foundation for the design of new\n                    <jats:styled-content style=\"fixed-case\">CELSR<\/jats:styled-content>\n                    \u2010targeted therapeutic reagents.\n                    <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                      <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc12955-fig-0005-m.png\">\n                        <jats:alt-text>image<\/jats:alt-text>\n                      <\/jats:graphic>\n                    <\/jats:boxed-text>\n                  <\/jats:p>\n                  <jats:p>The cadherin EGF LAG seven\u2010pass G\u2010type receptors (CELSRs) are a special subgroup of adhesion G protein\u2010coupled receptors (GPCRs), which have large ecto\u2010domains that form homophilic interactions and encompass more than 2000 amino acids. Recent studies have revealed that CELSRs are pivotal regulators of many biological processes, such as neuronal\/endocrine cell differentiation, vessel valve formation and the control of planar cell polarity during embryonic development.<\/jats:p>","DOI":"10.1111\/jnc.12955","type":"journal-article","created":{"date-parts":[[2014,10,3]],"date-time":"2014-10-03T12:03:30Z","timestamp":1412337810000},"page":"699-711","source":"Crossref","is-referenced-by-count":52,"title":["Understanding cadherin\n                    <scp>EGF LAG<\/scp>\n                    seven\u2010pass G\u2010type receptors"],"prefix":"10.1111","volume":"131","author":[{"given":"Xiao\u2010Jing","family":"Wang","sequence":"first","affiliation":[{"name":"Key Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology Shandong University School of Medicine Jinan Shandong China"},{"name":"Department of Cell Biology Shandong University School of Medicine Jinan 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