{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T21:10:57Z","timestamp":1760908257524,"version":"3.41.2"},"reference-count":13,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2006,3,15]]},"abstract":"<jats:p>The AMPK (AMP-activated protein kinase)-related protein kinase subfamily of the human kinome comprises 12 members closely related to the catalytic \u03b11\/\u03b12 subunits of AMPK. The precise role of the AMPK-related kinases and their in vivo substrates is rather unclear at present, but some are involved in regulating cell polarity, whereas others appear to control cellular differentiation. Of the 12 human AMPK-related protein kinase family members, 11 can be activated following phosphorylation of their T-loop threonine residue by the LKB1 complex. Nine of these AMPK-related kinases activated by LKB1 contain an UBA (ubiquitin-associated) domain immediately C-terminal to the kinase catalytic domain. In this issue of the Biochemical Journal, Jaleel et al. show that the presence of an UBA domain in AMP-related kinases allows LKB1-induced phosphorylation and activation. The findings have implications for understanding the molecular mechanisms of activation of this fascinating family of protein kinases. Also, mutations in the UBA domains of the AMP-related kinase genes might be present in families with Peutz\u2013Jehgers syndrome and in other cancer patients.<\/jats:p>","DOI":"10.1042\/bj20060184","type":"journal-article","created":{"date-parts":[[2006,3,2]],"date-time":"2006-03-02T09:11:08Z","timestamp":1141290668000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["The ubiquitin-associated domain of AMPK-related protein kinases allows LKB1-induced phosphorylation and activation"],"prefix":"10.1042","volume":"394","author":[{"given":"Mark\u00a0H.","family":"Rider","sequence":"first","affiliation":[{"name":"Hormone and Metabolic Research Unit, Christian de Duve Institute of Cellular Pathology and Universit\u00e9 catholique de Louvain, Avenue Hippocrate 75, B-1200 Brussels, Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2006,2,24]]},"reference":[{"key":"2021112214090136600_B1","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.cmet.2004.12.003","article-title":"AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism","volume":"1","author":"Kahn","year":"2005","journal-title":"Cell Metab."},{"key":"2021112214090136600_B2","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1126\/science.1107403","article-title":"Mammalian SAD kinases are required for neuronal polarization","volume":"307","author":"Kishi","year":"2005","journal-title":"Science"},{"key":"2021112214090136600_B3","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.tcb.2004.04.001","article-title":"LKB1 tumor suppressor protein: PARtaker in cell polarity","volume":"14","author":"Baas","year":"2004","journal-title":"Trends Cell Biol."},{"key":"2021112214090136600_B4","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.bbagen.2005.03.015","article-title":"Regulation of SNARK activity in response to cellular stresses","volume":"1724","author":"Lefebvre","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112214090136600_B5","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1186\/1475-4924-2-28","article-title":"Complexes between the LKB1 tumor suppressor, STRAD\u03b1\/\u03b2 and MO25\u03b1\/\u03b2 are upstream kinases in the AMP-activated protein kinase cascade","volume":"2","author":"Hawley","year":"2003","journal-title":"J. Biol."},{"key":"2021112214090136600_B6","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.1016\/j.cub.2003.10.031","article-title":"LKB1 is the upstream kinase in the AMP-activated protein kinase cascade","volume":"13","author":"Woods","year":"2003","journal-title":"Curr. Biol."},{"key":"2021112214090136600_B7","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1038\/sj.emboj.7600110","article-title":"LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK\/PAR-1","volume":"23","author":"Lizcano","year":"2004","journal-title":"EMBO J."},{"key":"2021112214090136600_B8","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1016\/j.febslet.2005.01.042","article-title":"Identification of the sucrose non-fermenting related kinase SNRK as a novel LKB1 substrate","volume":"579","author":"Jaleel","year":"2005","journal-title":"FEBS Lett."},{"key":"2021112214090136600_B9","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1042\/BJ20051844","article-title":"The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation","volume":"394","author":"Jaleel","year":"2006","journal-title":"Biochem. J."},{"key":"2021112214090136600_B10","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nrm1701","article-title":"Ubiquitin-binding domains","volume":"6","author":"Hicke","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021112214090136600_B11","doi-asserted-by":"crossref","first-page":"29060","DOI":"10.1074\/jbc.M503824200","article-title":"The Ca2+\/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases","volume":"280","author":"Hurley","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021112214090136600_B12","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.cmet.2005.05.009","article-title":"Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase","volume":"1","author":"Hawley","year":"2005","journal-title":"Cell Metab."},{"key":"2021112214090136600_B13","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.cmet.2005.06.005","article-title":"Ca2+\/calmodulin-dependent protein kinase kinase-\u03b2 acts upstream of AMP-activated protein kinase in mammalian cells","volume":"1","author":"Woods","year":"2005","journal-title":"Cell Metab."}],"container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/doi\/10.1042\/BJ20060184\/641424\/bj394e007.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/doi\/10.1042\/BJ20060184\/641424\/bj394e007.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T16:40:10Z","timestamp":1637599210000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/394\/3\/e7\/44101\/The-ubiquitin-associated-domain-of-AMPK-related"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,2,24]]},"references-count":13,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2006,3,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20060184","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"type":"print","value":"0264-6021"},{"type":"electronic","value":"1470-8728"}],"subject":[],"published":{"date-parts":[[2006,2,24]]},"article-number":"e7"}}