{"id":118,"date":"2012-12-03T10:14:27","date_gmt":"2012-12-03T14:14:27","guid":{"rendered":"http:\/\/blog.uvm.edu\/dwarshaw\/?page_id=118"},"modified":"2017-08-09T16:09:15","modified_gmt":"2017-08-09T16:09:15","slug":"myosin-binding-protein-c-mybp-c","status":"publish","type":"page","link":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/research-interests\/myosin-binding-protein-c-mybp-c\/","title":{"rendered":"Myosin Binding Protein-C (MyBP-C)"},"content":{"rendered":"\n\n\n
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RESEARCH INTERESTS<\/h4>\n

Myosin Binding Protein-C (MyBP-C)<\/h1>\n

MyBP-C is a striated muscle contractile protein, mutations to which have been linked to genetic forms of hypertrophic and dilated cardiomyopathies as well as skeletal muscle myopathies (i.e. distal arthrogryposis). MyBP-C is expressed as 3 isoforms; fast skeletal, slow skeletal, and cardiac. It\u2019s an elongated protein with at least 10 globular domains (yellow structures). MyBP-C associates with the myosin thick filament at one end and both the myosin head region and actin at its other end.
\n\"\"<\/a>Striated muscles are composed of repeating contractile units called sarcomeres in which the thin, actin-containing and thick, myosin-containing filaments overlap and slide past each other during muscle shortening. The myosin thick filament is composed of 300 myosin molecules that form a bipolar filament in which the myosin heads on each half of the thick filament are oriented to move the thin filament towards the center of the sarcomere. Interestingly, MyBP-C is localized to two regions (C-zones) near the center of the thick filament and thus the sarcomere. Why is MyBP-C localized to only these discrete zones is a major lab interest?<\/p>\n

\"\"<\/a>Although MyBP-C affects actomyosin function, the molecular mechanism by which this occurs is far from certain, with multiple models proposed for its action. The specific model depends on MyBP-C\u2019s binding partner. For example, by binding to the myosin head region, MyBP-C may limit myosin\u2019s interaction with actin and maintain myosin in a super-relaxed state. Alternatively, MyBP-C may bind to actin and act as an internal load to shortening or activate the thin filament in a calcium-independent manner.<\/p>\n

\"\"<\/a>Our laboratory uses molecular biophysics to unravel the key interactions between MyBP-C and both actin and myosin that allow this unique protein to modulate actomyosin function in the heart and in skeletal muscles.<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

<\/p>\n","protected":false},"excerpt":{"rendered":"

RESEARCH INTERESTS Myosin Binding Protein-C (MyBP-C) MyBP-C is a striated muscle contractile protein, mutations to which have been linked to genetic forms of hypertrophic and dilated cardiomyopathies as well as skeletal muscle myopathies (i.e. distal arthrogryposis). MyBP-C is expressed as … Continue reading →<\/span><\/a><\/p>\n","protected":false},"author":3,"featured_media":0,"parent":13,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"sidebar-page.php","meta":[],"_links":{"self":[{"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/pages\/118"}],"collection":[{"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/comments?post=118"}],"version-history":[{"count":11,"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/pages\/118\/revisions"}],"predecessor-version":[{"id":780,"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/pages\/118\/revisions\/780"}],"up":[{"embeddable":true,"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/pages\/13"}],"wp:attachment":[{"href":"https:\/\/physioweb.uvm.edu\/warshaw-lab\/wp-json\/wp\/v2\/media?parent=118"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}