{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T20:30:51Z","timestamp":1718656251936},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1989,10,1]]},"abstract":"<jats:p>A protein kinase activity was identified in pig brain that co-purified with microtubules through repeated cycles of temperature-dependent assembly and disassembly. The microtubule-associated protein kinase (MTAK) phosphorylated histone H1; this activity was not stimulated by cyclic nucleotides. Ca2+ plus calmodulin, phospholipids or polyamines. MTAK did not phosphorylate synthetic peptides which are substrates for cyclic AMP-dependent protein kinase, cyclic GMP-dependent protein kinase. Ca2+\/calmodulin-dependent protein kinase II, protein kinase C or casein kinase II. MTAK activity was inhibited by trifluoperazine [IC50 (median inhibitory concn.) = 600 microM] in a Ca2+-independent fashion. Ca2+ alone was inhibitory [IC50 = 4 mM). MTAK was not inhibited by heparin, a potent inhibitor of casein kinase II, nor a synthetic peptide inhibitor of cyclic AMP-dependent protein kinase. MTAK demonstrated a broad pH maximum (7.5-8.5) and an apparent Km for ATP of 45 microM. Mg2+ was required for enzyme activity and could not be replaced by Mn2+. MTAK phosphorylated serine and threonine residues on histone H1. MTAK is a unique cofactor-independent protein kinase that binds to microtubule structures.<\/jats:p>","DOI":"10.1042\/bj2630207","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:14:21Z","timestamp":1439241261000},"page":"207-214","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Properties of a microtubule-associated cofactor-independent protein kinase from pig brain"],"prefix":"10.1042","volume":"263","author":[{"given":"C W","family":"Scott","sequence":"first","affiliation":[{"name":"Department of Pharmacology, ICI Pharmaceuticals Group, ICI Americas, Wilmington, DE 19897, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C B","family":"Caputo","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, ICI Pharmaceuticals Group, ICI Americas, Wilmington, DE 19897, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A I","family":"Salama","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, ICI Pharmaceuticals Group, ICI Americas, Wilmington, DE 19897, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/263\/1\/207\/598225\/bj2630207.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/263\/1\/207\/598225\/bj2630207.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:08:36Z","timestamp":1637863716000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/263\/1\/207\/24483\/Properties-of-a-microtubule-associated-cofactor"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1989,10,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1989,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2630207","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1989,10,1]]}}}