{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T03:45:36Z","timestamp":1772768736883,"version":"3.50.1"},"reference-count":42,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2002,1,4]],"date-time":"2002-01-04T00:00:00Z","timestamp":1010102400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2002,2,20]]},"abstract":"<jats:p>Spectrin repeats are three\u2010helix bundle structures which occur in a large number of diverse proteins, either as single copies or in tandem arrangements of multiple repeats. They can serve structural purposes, by coordination of cytoskeletal interactions with high spatial precision, as well as a \u2018switchboard\u2019 for interactions with multiple proteins with a more regulatory role. We describe the structure of the \u03b1\u2010actinin spectrin repeats as a prototypical example, their assembly in a defined antiparallel dimer, and the interactions of spectrin repeats with multiple other proteins. The \u03b1\u2010actinin rod domain shares several features common to other spectrin repeats. (1) The rod domain forms a rigid connection between two actin\u2010binding domains positioned at the two ends of the \u03b1\u2010actinin dimer. The exact distance and rigidity are important, for example, for organizing the muscle Z\u2010line and maintaining its architecture during muscle contraction. (2) The spectrin repeats of \u03b1\u2010actinin have evolved to make tight antiparallel homodimer contacts. (3) The spectrin repeats are important interaction sites for multiple structural and signalling proteins. The interactions of spectrin repeats are, however, diverse and defy any simple classification of their preferred interaction sites, which is possible for other domains (e.g. src\u2010homology domains 3 or 2). Nevertheless, the binding properties of the repeats perform important roles in the biology of the proteins where they are found, and lead to the assembly of complex, multiprotein structures involved both in cytoskeletal architecture as well as in forming large signal transduction complexes.<\/jats:p>","DOI":"10.1016\/s0014-5793(01)03304-x","type":"journal-article","created":{"date-parts":[[2002,10,14]],"date-time":"2002-10-14T15:56:01Z","timestamp":1034610961000},"page":"119-123","source":"Crossref","is-referenced-by-count":249,"title":["The spectrin repeat: a structural platform for cytoskeletal protein assemblies"],"prefix":"10.1002","volume":"513","author":[{"given":"Kristina","family":"Djinovic-Carugo","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mathias","family":"Gautel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jari","family":"Yl\u00e4nne","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul","family":"Young","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2002,1,4]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1018627705273"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(00)01704-X"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81980-7"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.8446897"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/bies.950190911"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81981-9"},{"key":"e_1_2_7_8_1","first-page":"234","volume":"6","author":"Yl\u00e4nne J","year":"2001","journal-title":"Cell Mol. 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