{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T01:49:32Z","timestamp":1774921772355,"version":"3.50.1"},"reference-count":46,"publisher":"Rockefeller University Press","issue":"6","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2001,9,17]]},"abstract":"<jats:p>Huntingtin-interacting protein 1 related (Hip1R) is a novel component of clathrin-coated pits and vesicles and is a mammalian homologue of Sla2p, an actin-binding protein important for both actin organization and endocytosis in yeast. Here, we demonstrate that Hip1R binds via its putative central coiled-coil domain to clathrin, and provide evidence that Hip1R and clathrin are associated in vivo at sites of endocytosis. First, real-time analysis of Hip1R\u2013YFP and DsRed\u2013clathrin light chain (LC) in live cells revealed that these proteins show almost identical temporal and spatial regulation at the cell cortex. Second, at the ultrastructure level, immunogold labeling of \u2018unroofed\u2019 cells showed that Hip1R localizes to clathrin-coated pits. Third, overexpression of Hip1R affected the subcellular distribution of clathrin LC. Consistent with a functional role for Hip1R in endocytosis, we also demonstrated that it promotes clathrin cage assembly in vitro. Finally, we showed that Hip1R is a rod-shaped apparent dimer with globular heads at either end, and that it can assemble clathrin-coated vesicles and F-actin into higher order structures. In total, Hip1R's properties suggest an early endocytic function at the interface between clathrin, F-actin, and lipids.<\/jats:p>","DOI":"10.1083\/jcb.200106089","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:46:23Z","timestamp":1027701983000},"page":"1209-1224","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":217,"title":["The actin-binding protein Hip1R associates with clathrin during early stages of endocytosis and promotes clathrin assembly in vitro"],"prefix":"10.1083","volume":"154","author":[{"given":"A\u030asa E.Y.","family":"Engqvist-Goldstein","sequence":"first","affiliation":[{"name":"1Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720"}]},{"given":"Robin A.","family":"Warren","sequence":"additional","affiliation":[{"name":"2Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107"}]},{"given":"Michael M.","family":"Kessels","sequence":"additional","affiliation":[{"name":"3Department of Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, D-39008 Magdeburg, Germany"}]},{"given":"James H.","family":"Keen","sequence":"additional","affiliation":[{"name":"2Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, PA 19107"}]},{"given":"John","family":"Heuser","sequence":"additional","affiliation":[{"name":"4Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63130"}]},{"given":"David G.","family":"Drubin","sequence":"additional","affiliation":[{"name":"1Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720"}]}],"member":"291","published-online":{"date-parts":[[2001,9,17]]},"reference":[{"key":"2023072214284468400_BIB1","doi-asserted-by":"crossref","first-page":"3143","DOI":"10.1002\/j.1460-2075.1986.tb04621.x","volume":"5","year":"1986","journal-title":"EMBO J"},{"key":"2023072214284468400_BIB2","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1083\/jcb.111.1.19","volume":"111","year":"1990","journal-title":"J. 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