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The domains are persistent but readily exchange components with their surroundings, and their formation is dependent on the number of Nck SH3 domains, suggesting they are phase separated polymers assembled through multivalent interactions among the three proteins. The domains form independent of the actin cytoskeleton, but acto-myosin contractility induces their rapid lateral movement. Nephrin phosphorylation induces larger clusters at the cell periphery, which are associated with extensive actin assembly and dense filopodia. Our studies illustrate how multivalent interactions between proteins at the plasma membrane can produce micron-scale organization of signaling molecules, and how the resulting clusters can both respond to and control the actin cytoskeleton.<\/jats:p>","DOI":"10.1091\/mbc.e18-12-0823","type":"journal-article","created":{"date-parts":[[2019,10,10]],"date-time":"2019-10-10T09:45:37Z","timestamp":1570700737000},"page":"2996-3012","source":"Crossref","is-referenced-by-count":42,"title":["Phosphorylation of nephrin induces phase separated domains that move through actomyosin contraction"],"prefix":"10.1091","volume":"30","author":[{"given":"Soyeon","family":"Kim","sequence":"first","affiliation":[{"name":"Department of Biophysics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390"},{"name":"The HHMI\/MBL Summer Institute, Marine Biological Laboratory, Woods Hole, MA 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