{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T17:21:06Z","timestamp":1774286466465,"version":"3.50.1"},"reference-count":28,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":4052,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Motil. Cytoskeleton"],"published-print":{"date-parts":[[1994,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>High molecular weight microtubule\u2010associated proteins MAP1A and MAP2 form thin projections from microtubule surfaces and have been implicated in crosslinking microtubules and other cytoskeletal components. We have purified native MAP1A from bovine brain and have studied its interaction with G\u2010 and F\u2010actin. Using a solid\u2010phase immunoassay we show that MAP1A binds in a dose\u2010dependent manner to both G\u2010actin and F\u2010actin. Addition of MAP1A to F\u2010actin causes gelation of F\u2010actin and SDS\u2010PAGE analysis shows that MAP1A co\u2010sediments with the gelled network, under conditions where F\u2010actin alone does not pellet. The low apparent viscosity of F\u2010actin is markedly increased in the presence of MAP1A, suggesting that MAP1A can crosslink F\u2010actin. Co\u2010incubation experiments indicate that MAP1A and MAP2 may bind to common or overlapping sites on the actin molecule. The widespread distribution of MAP1A and its interaction with microtubules, actin, and intermediate filaments suggests that it may constitute an important determinant of neuronal and non\u2010neuronal cellular morphology. \u00a9 1994 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/cm.970290203","type":"journal-article","created":{"date-parts":[[2005,2,24]],"date-time":"2005-02-24T01:54:54Z","timestamp":1109210094000},"page":"110-116","source":"Crossref","is-referenced-by-count":55,"title":["Microtubule associated protein MAP1A is an actin\u2010binding and crosslinking protein"],"prefix":"10.1002","volume":"29","author":[{"given":"Barbara","family":"Pedrotti","sequence":"first","affiliation":[]},{"given":"Roberto","family":"Colombo","sequence":"additional","affiliation":[]},{"given":"Khalid","family":"Islam","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2005,2,4]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.82.5.1434"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1984.tb08235.x"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/360674a0"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj2690061"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.78.3.958"},{"key":"e_1_2_1_7_1","doi-asserted-by":"crossref","first-page":"9135","DOI":"10.1016\/S0021-9258(18)34253-4","article-title":"Cross\u2010linking of actin filament networks by self\u2010association and actin\u2010binding macro\u2010molecules","volume":"257","author":"Griffith L. 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Biochemistry (in press).","DOI":"10.1021\/bi00195a023"},{"key":"e_1_2_1_20_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00356a025"},{"key":"e_1_2_1_21_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.90.2.467"},{"key":"e_1_2_1_22_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1749-6632.1986.tb38464.x"},{"key":"e_1_2_1_23_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.78.7.4329"},{"key":"e_1_2_1_24_1","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1523\/JNEUROSCI.07-05-01461.1987","article-title":"The molecular structure of microtubule\u2010associated protein MAP1A in vitro and in vivo. An immunoelectron microscopy and quick\u2010freeze, deep\u2010etch study","volume":"7","author":"Shiomura Y.","year":"1987","journal-title":"J. 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