Swiprosin-1 Is a Novel Actin Bundling Protein That Regulates Cell Spreading and Migration

Authors
Kwon, Min-SungPark, Kyoung RyoungKim, Young-DaeNa, Bo-RaKim, Hye-RanChoi, Hak-JongPiragyte, IndreJeon, HyesungChung, Kyung HwunSong, Woo KeunEom, Soo HyunJun, Chang-Duk
Issue Date
2013-08
Publisher
PUBLIC LIBRARY SCIENCE
Citation
PLOS ONE, v.8, no.8
Abstract
Protein functions are often revealed by their localization to specialized cellular sites. Recent reports demonstrated that swiprosin-1 is found together with actin and actin-binding proteins in the cytoskeleton fraction of human mast cells and NK-like cells. However, direct evidence of whether swiprosin-1 regulates actin dynamics is currently lacking. We found that swiprosin-1 localizes to microvilli-like membrane protrusions and lamellipodia and exhibits actin-binding activity. Overexpression of swiprosin-1 enhanced lamellipodia formation and cell spreading. In contrast, swiprosin-1 knockdown showed reduced cell spreading and migration. Swiprosin-1 induced actin bundling in the presence of Ca2+, and deletion of the EF-hand motifs partially reduced bundling activity. Swiprosin-1 dimerized in the presence of Ca2+ via its coiled-coil domain, and a lysine (Lys)-rich region in the coiled-coil domain was essential for regulation of actin bundling. Consistent with these observations, mutations of the EF-hand motifs and coiled-coil region significantly reduced cell spreading and lamellipodia formation. We provide new evidence of how swiprosin-1 influences cytoskeleton reorganization and cell spreading.
Keywords
CROSS-LINKING; BINDING PROTEIN; ARP2/3 COMPLEX; MEMBRANE PROTRUSION; HUMAN FASCIN; EF-HAND; F-ACTIN; PHOSPHORYLATION; IDENTIFICATION; DOMAIN
ISSN
1932-6203
URI
https://pubs.kist.re.kr/handle/201004/127789
DOI
10.1371/journal.pone.0071626
Appears in Collections:
KIST Article > 2013
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