{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T02:34:56Z","timestamp":1791513296101,"version":"4.3.4"},"reference-count":69,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2023,9,15]],"date-time":"2023-09-15T00:00:00Z","timestamp":1694736000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35\u2010GM140631"],"award-info":[{"award-number":["R35\u2010GM140631"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Cytoskeleton"],"published-print":{"date-parts":[[2024,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The dynein\u2010driven beating of cilia is required to move individual cells and to generate fluid flow across surfaces and within cavities. These motor enzymes are highly complex and can contain upwards of 20 different protein components with a total mass approaching 2\u2009MDa. The dynein heavy chains are enormous proteins consisting of ~4500 residues and ribosomes take approximately 15\u2009min to synthesize one. Studies in a broad array of organisms ranging from the green alga <jats:italic>Chlamydomonas<\/jats:italic> to humans has identified 19 cytosolic factors (DNAAFs) that are needed to specifically build axonemal dyneins; defects in many of these proteins lead to primary ciliary dyskinesia in mammals which can result in infertility, severe bronchial problems, and <jats:italic>situs inversus<\/jats:italic>. How all these factors cooperate in a spatially and temporally regulated manner to promote dynein assembly in cytoplasm remains very uncertain. These DNAAFs contain a variety of well\u2010folded domains many of which provide protein interaction surfaces. However, many also exhibit large regions that are predicted to be inherently disordered. Here I discuss the nature of these unstructured segments, their predicted propensity for driving protein phase separation, and their potential for adopting more defined conformations during the dynein assembly process.<\/jats:p>","DOI":"10.1002\/cm.21789","type":"journal-article","created":{"date-parts":[[2023,9,15]],"date-time":"2023-09-15T11:27:44Z","timestamp":1694777264000},"page":"515-528","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Inherently disordered regions of axonemal dynein assembly factors"],"prefix":"10.1002","volume":"81","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5484-5530","authenticated-orcid":false,"given":"Stephen M.","family":"King","sequence":"first","affiliation":[{"name":"Department of Molecular Biology and Biophysics University of Connecticut Health Center  Farmington Connecticut USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2023,9,15]]},"reference":[{"key":"e_1_2_14_2_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200802025"},{"key":"e_1_2_14_3_1","doi-asserted-by":"publisher","DOI":"10.1042\/BST20160172"},{"key":"e_1_2_14_4_1","doi-asserted-by":"publisher","DOI":"10.1038\/nphys3532"},{"key":"e_1_2_14_5_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.202109014"},{"key":"e_1_2_14_6_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.201011152"},{"key":"e_1_2_14_7_1","doi-asserted-by":"publisher","DOI":"10.1002\/cm.21206"},{"key":"e_1_2_14_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ajhg.2009.11.008"},{"key":"e_1_2_14_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-25413-w"},{"key":"e_1_2_14_10_1","doi-asserted-by":"publisher","DOI":"10.3390\/cells4030500"},{"key":"e_1_2_14_11_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00401-022-02463-y"},{"key":"e_1_2_14_12_1","doi-asserted-by":"publisher","DOI":"10.1038\/nrm2278"},{"key":"e_1_2_14_13_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkad214"},{"key":"e_1_2_14_14_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41477-020-00811-y"},{"key":"e_1_2_14_15_1","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.38497"},{"key":"e_1_2_14_16_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-cellbio-100913-013325"},{"key":"e_1_2_14_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2022.102801"},{"key":"e_1_2_14_18_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41586-021-03819-2"},{"key":"e_1_2_14_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2011.08.016"},{"key":"e_1_2_14_20_1","doi-asserted-by":"publisher","DOI":"10.1186\/s12964-023-01135-y"},{"key":"e_1_2_14_21_1","doi-asserted-by":"publisher","DOI":"10.1002\/cm.20129"},{"key":"e_1_2_14_22_1","first-page":"163","volume-title":"Dyneins: Structure, biology and disease","author":"King S. 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