Doubling up on function: dual-specificity tyrosine-regulated kinase 1A
DYRK1A, the dual-specificity kinase, is again doubling up on function, as reported by Bhansali, Rammohan, and colleagues in this issue of the JCI. DYRK1A is an evolutionarily conserved protein kinase with dual specificity; it adds phosphates to serine/threonine residues of diverse regulatory protein...
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Veröffentlicht in: | The Journal of clinical investigation 2021-01, Vol.131 (1) |
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creator | Kim, Jung-Hyun Li, Liping Resar, Linda M.S |
description | DYRK1A, the dual-specificity kinase, is again doubling up on function, as reported by Bhansali, Rammohan, and colleagues in this issue of the JCI. DYRK1A is an evolutionarily conserved protein kinase with dual specificity; it adds phosphates to serine/threonine residues of diverse regulatory proteins and activates its own function by autophosphorylating a critical tyrosine at position 321 in the activation loop. Bhansali, Rammohan, and colleagues investigated B cell acute lymphoblastic leukemia (B-ALL) in individuals with Down syndrome (DS) and in children with leukemia characterized by aneuploidy. The study revealed a DYRK1A/FOXO1 and STAT3 signaling pathway in B-ALL that could be targeted pharmacologically, thus opening the door to therapeutic strategies for patients with leukemia with or without DS. |
doi_str_mv | 10.1172/JCI142627 |
format | Article |
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DYRK1A is an evolutionarily conserved protein kinase with dual specificity; it adds phosphates to serine/threonine residues of diverse regulatory proteins and activates its own function by autophosphorylating a critical tyrosine at position 321 in the activation loop. Bhansali, Rammohan, and colleagues investigated B cell acute lymphoblastic leukemia (B-ALL) in individuals with Down syndrome (DS) and in children with leukemia characterized by aneuploidy. The study revealed a DYRK1A/FOXO1 and STAT3 signaling pathway in B-ALL that could be targeted pharmacologically, thus opening the door to therapeutic strategies for patients with leukemia with or without DS.</description><identifier>ISSN: 0021-9738</identifier><identifier>EISSN: 1558-8238</identifier><identifier>DOI: 10.1172/JCI142627</identifier><language>eng</language><publisher>American Society for Clinical Investigation</publisher><subject>Acute lymphocytic leukemia ; Care and treatment ; Development and progression ; Enzymes ; Genetic aspects ; Health aspects ; Phosphotransferases ; Regulation</subject><ispartof>The Journal of clinical investigation, 2021-01, Vol.131 (1)</ispartof><rights>COPYRIGHT 2021 American Society for Clinical Investigation</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids></links><search><creatorcontrib>Kim, Jung-Hyun</creatorcontrib><creatorcontrib>Li, Liping</creatorcontrib><creatorcontrib>Resar, Linda M.S</creatorcontrib><title>Doubling up on function: dual-specificity tyrosine-regulated kinase 1A</title><title>The Journal of clinical investigation</title><description>DYRK1A, the dual-specificity kinase, is again doubling up on function, as reported by Bhansali, Rammohan, and colleagues in this issue of the JCI. DYRK1A is an evolutionarily conserved protein kinase with dual specificity; it adds phosphates to serine/threonine residues of diverse regulatory proteins and activates its own function by autophosphorylating a critical tyrosine at position 321 in the activation loop. Bhansali, Rammohan, and colleagues investigated B cell acute lymphoblastic leukemia (B-ALL) in individuals with Down syndrome (DS) and in children with leukemia characterized by aneuploidy. The study revealed a DYRK1A/FOXO1 and STAT3 signaling pathway in B-ALL that could be targeted pharmacologically, thus opening the door to therapeutic strategies for patients with leukemia with or without DS.</description><subject>Acute lymphocytic leukemia</subject><subject>Care and treatment</subject><subject>Development and progression</subject><subject>Enzymes</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>Phosphotransferases</subject><subject>Regulation</subject><issn>0021-9738</issn><issn>1558-8238</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNqF0DFLAzEcBfAgCtbq4DfIJDicJrnkknMr1WqlUNDiWv7JJddoyBWTgP32KjrUybe85ccbHkLnlFxRKtn143ROOWuYPEAjKoSqFKvVIRoRwmjVylodo5OUXgmhnAs-QrPboejgY4_LFg8RuxJN9kO8wV2BUKWtNd554_MO5937kHy01bvtS4BsO_zmIySL6eQUHTkIyZ799hitZner6UO1WN7Pp5NF1bctryxvmwYIVcToThArlbCaNwSobq3pgNfAtZNfAQ1Ot1Qa5gQw44QmtVH1GF3-zPYQ7NpHM8RsP3IPJaX1_PlpPWm4lFwJyv-xy5e_9mLPbiyEvElDKN9PpH34Ce2waS4</recordid><startdate>20210101</startdate><enddate>20210101</enddate><creator>Kim, Jung-Hyun</creator><creator>Li, Liping</creator><creator>Resar, Linda M.S</creator><general>American Society for Clinical Investigation</general><scope>IOV</scope><scope>ISR</scope></search><sort><creationdate>20210101</creationdate><title>Doubling up on function: dual-specificity tyrosine-regulated kinase 1A</title><author>Kim, Jung-Hyun ; Li, Liping ; Resar, Linda M.S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g994-e4966a0180cbd50e785eb460a1b9ecda43a4bf7777abafb917c2f5a2cf5b03c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Acute lymphocytic leukemia</topic><topic>Care and treatment</topic><topic>Development and progression</topic><topic>Enzymes</topic><topic>Genetic aspects</topic><topic>Health aspects</topic><topic>Phosphotransferases</topic><topic>Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Jung-Hyun</creatorcontrib><creatorcontrib>Li, Liping</creatorcontrib><creatorcontrib>Resar, Linda M.S</creatorcontrib><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><jtitle>The Journal of clinical investigation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Jung-Hyun</au><au>Li, Liping</au><au>Resar, Linda M.S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Doubling up on function: dual-specificity tyrosine-regulated kinase 1A</atitle><jtitle>The Journal of clinical investigation</jtitle><date>2021-01-01</date><risdate>2021</risdate><volume>131</volume><issue>1</issue><issn>0021-9738</issn><eissn>1558-8238</eissn><abstract>DYRK1A, the dual-specificity kinase, is again doubling up on function, as reported by Bhansali, Rammohan, and colleagues in this issue of the JCI. DYRK1A is an evolutionarily conserved protein kinase with dual specificity; it adds phosphates to serine/threonine residues of diverse regulatory proteins and activates its own function by autophosphorylating a critical tyrosine at position 321 in the activation loop. Bhansali, Rammohan, and colleagues investigated B cell acute lymphoblastic leukemia (B-ALL) in individuals with Down syndrome (DS) and in children with leukemia characterized by aneuploidy. The study revealed a DYRK1A/FOXO1 and STAT3 signaling pathway in B-ALL that could be targeted pharmacologically, thus opening the door to therapeutic strategies for patients with leukemia with or without DS.</abstract><pub>American Society for Clinical Investigation</pub><doi>10.1172/JCI142627</doi></addata></record> |
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source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
subjects | Acute lymphocytic leukemia Care and treatment Development and progression Enzymes Genetic aspects Health aspects Phosphotransferases Regulation |
title | Doubling up on function: dual-specificity tyrosine-regulated kinase 1A |
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