{"id":5078,"date":"2014-10-22T10:47:20","date_gmt":"2014-10-22T14:47:20","guid":{"rendered":"https:\/\/web.uri.edu\/inbre\/?page_id=5078"},"modified":"2014-10-22T10:47:20","modified_gmt":"2014-10-22T14:47:20","slug":"zhang","status":"publish","type":"page","link":"https:\/\/web.uri.edu\/riinbre\/research\/zhang\/","title":{"rendered":"Classification and Functional Characterization of the PP1-binding Proteins"},"content":{"rendered":"<p><strong>Investigator:<\/strong> \u00a0Ying Zhang, University of Rhode Island<\/p>\n<p><strong>Mentor:<\/strong> \u00a0Rebecca Page, Brown University<\/p>\n<p><strong>Scientific Theme:<\/strong> \u00a0Neuroscience &amp; Cancer<\/p>\n<p style=\"text-align: justify\"><strong>Abstract:<\/strong> \u00a0The serine\/threonine protein phosphatase 1 (PP1) catalyzes the dephosphorylation of hundreds of protein\u00a0targets, including many key molecules in tumor suppression, neuronal signaling, and the regulation of\u00a0various cellular processes. Despite their substrate promiscuity, PP1 activity in the cell is rather specific and is\u00a0tightly regulated by its interaction with hundreds of PP1 regulatory proteins. Thus, one primary challenge in\u00a0the PP1 research is to understand how their functional specificity is mediated by the binding of diverse\u00a0regulators. Over the past few years, structural determination of at least eight PP1 holoenzymes has\u00a0provided significant insights into the interactions between PP1 and PP1 regulators, according to which up to\u00a0ten binding motifs has been identified. However, the experimentally determination of PP1 holoenzyme\u00a0structures is challenging. A comprehensive understanding is currently still lacking on the diversity of PP1-binding proteins and the usage of PP1-binding motifs. In the proposed project, we aim to solve this problem\u00a0by developing a computational procedure for a broader survey of the diversity and distribution of PP1-binding\u00a0proteins. This computational procedure will take advantage of the knowledge obtained from structural-based\u00a0studies and extend our understanding into the function of many other PP1 holoenzymes through sequencebased\u00a0identifications. The proposed study will set the stage for the identification of novel PP1-binding\u00a0proteins and novel regulatory mechanisms, which will be the focus of future funding applications to the NIH\u00a0and other agencies.<\/p>\n<p style=\"text-align: justify\"><strong>Human Health Relevance:<\/strong> \u00a0The proposed project will facilitate the construction of a preliminary data set and a preliminary protocol for the study of PP1, a functionally essential serine\/threonine phosphatase that participates in the regulation of a\u00a0plethora of pathological processes, including cancer, neurodegenerative diseases, type 2 diabetes, heart\u00a0failure and viral diseases.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Investigator: \u00a0Ying Zhang, University of Rhode Island Mentor: \u00a0Rebecca Page, Brown University Scientific Theme: \u00a0Neuroscience &amp; Cancer Abstract: \u00a0The serine\/threonine protein phosphatase 1 (PP1) catalyzes the dephosphorylation of hundreds of protein\u00a0targets, including many key molecules in tumor suppression, neuronal signaling, and the regulation of\u00a0various cellular processes. Despite their substrate promiscuity, PP1 activity in the cell [&hellip;]<\/p>\n","protected":false},"author":1036,"featured_media":0,"parent":40,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":"","_links_to":"","_links_to_target":""},"class_list":["post-5078","page","type-page","status-publish","hentry"],"acf":[],"_links":{"self":[{"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/pages\/5078","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/users\/1036"}],"replies":[{"embeddable":true,"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/comments?post=5078"}],"version-history":[{"count":0,"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/pages\/5078\/revisions"}],"up":[{"embeddable":true,"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/pages\/40"}],"wp:attachment":[{"href":"https:\/\/web.uri.edu\/riinbre\/wp-json\/wp\/v2\/media?parent=5078"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}