{"id":123,"date":"2012-11-19T16:33:18","date_gmt":"2012-11-19T21:33:18","guid":{"rendered":"https:\/\/sites.bu.edu\/morgan-lab\/?page_id=123"},"modified":"2021-06-09T13:46:11","modified_gmt":"2021-06-09T17:46:11","slug":"caldesmon","status":"publish","type":"page","link":"https:\/\/sites.bu.edu\/morgan-lab\/topics-of-interest\/caldesmon\/","title":{"rendered":"Caldesmon (CaD)"},"content":{"rendered":"<p><a href=\"\/morgan-lab\/files\/2012\/11\/caldesmon.jpg\"><img loading=\"lazy\" src=\"\/morgan-lab\/files\/2012\/11\/caldesmon.jpg\" alt=\"Caldesmon\" title=\"Caldesmon\" class=\"alignleft size-full wp-image-125\" height=\"539\" width=\"719\" srcset=\"https:\/\/sites.bu.edu\/morgan-lab\/files\/2012\/11\/caldesmon.jpg 719w, https:\/\/sites.bu.edu\/morgan-lab\/files\/2012\/11\/caldesmon-636x476.jpg 636w\" sizes=\"(max-width: 719px) 100vw, 719px\" \/><\/a><\/p>\n<p>&nbsp;<\/p>\n<p>Caldesmon is an actin and tropomyosin binding proten. It can be a substrate for ERK1\/2. We have hypothesized that the C-terminal end of CaD binds actin and blocks actin-myosin interactions until the phosphorylation of CaD by ERK.This phosphorylation is proposed to cause a conformational change (exaggerated in diagram) which allows increased actin-myosin interactions. The N-terminal end of CaD is thought to tether CaD (and the attached actin) to myosin. Disruption of this tethering with an N-terminal CaD peptide disrupts the placement of the C-terminal end of CaD relative to the myosin head and improves actin-myosin interactions. [Lee et al 1999]<\/p>\n<p><a href=\"\/morgan-lab\/files\/2012\/11\/signaling_cascade.jpg\"><img loading=\"lazy\" src=\"\/morgan-lab\/files\/2012\/11\/signaling_cascade.jpg\" alt=\"&quot;Signaling Cascade Diagram by Gangopadhay&amp;amp; Morgan, AJP :Cell, 2000&quot;\" title=\"&quot;Signaling Cascade Diagram by Gangopadhay&amp; Morgan, AJP :Cell, 2000&quot;\" class=\"alignleft size-full wp-image-126\" height=\"526\" width=\"463\" \/><\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>&nbsp; Caldesmon is an actin and tropomyosin binding proten. It can be a substrate for ERK1\/2. We have hypothesized that the C-terminal end of CaD binds actin and blocks actin-myosin interactions until the phosphorylation of CaD by ERK.This phosphorylation is proposed to cause a conformational change (exaggerated in diagram) which allows increased actin-myosin interactions. The [&hellip;]<\/p>\n","protected":false},"author":1251,"featured_media":0,"parent":602,"menu_order":3,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/pages\/123"}],"collection":[{"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/users\/1251"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/comments?post=123"}],"version-history":[{"count":5,"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/pages\/123\/revisions"}],"predecessor-version":[{"id":629,"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/pages\/123\/revisions\/629"}],"up":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/pages\/602"}],"wp:attachment":[{"href":"https:\/\/sites.bu.edu\/morgan-lab\/wp-json\/wp\/v2\/media?parent=123"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}