Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.

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 swipr...

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Autores principales:	Min-Sung Kwon, Kyoung Ryoung Park, Young-Dae Kim, Bo-Ra Na, Hye-Ran Kim, Hak-Jong Choi, Indre Piragyte, Hyesung Jeon, Kyung Hwun Chung, Woo Keun Song, Soo Hyun Eom, Chang-Duk Jun
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7351091967914947a9ffcb3ab1133653
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spelling	oai:doaj.org-article:7351091967914947a9ffcb3ab11336532021-11-18T08:59:25ZSwiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.1932-620310.1371/journal.pone.0071626https://doaj.org/article/7351091967914947a9ffcb3ab11336532013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23977092/?tool=EBIhttps://doaj.org/toc/1932-6203Protein 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 Ca(2+), and deletion of the EF-hand motifs partially reduced bundling activity. Swiprosin-1 dimerized in the presence of Ca(2+) 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.Min-Sung KwonKyoung Ryoung ParkYoung-Dae KimBo-Ra NaHye-Ran KimHak-Jong ChoiIndre PiragyteHyesung JeonKyung Hwun ChungWoo Keun SongSoo Hyun EomChang-Duk JunPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 8, p e71626 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Min-Sung Kwon Kyoung Ryoung Park Young-Dae Kim Bo-Ra Na Hye-Ran Kim Hak-Jong Choi Indre Piragyte Hyesung Jeon Kyung Hwun Chung Woo Keun Song Soo Hyun Eom Chang-Duk Jun Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
description	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 Ca(2+), and deletion of the EF-hand motifs partially reduced bundling activity. Swiprosin-1 dimerized in the presence of Ca(2+) 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.
format	article
author	Min-Sung Kwon Kyoung Ryoung Park Young-Dae Kim Bo-Ra Na Hye-Ran Kim Hak-Jong Choi Indre Piragyte Hyesung Jeon Kyung Hwun Chung Woo Keun Song Soo Hyun Eom Chang-Duk Jun
author_facet	Min-Sung Kwon Kyoung Ryoung Park Young-Dae Kim Bo-Ra Na Hye-Ran Kim Hak-Jong Choi Indre Piragyte Hyesung Jeon Kyung Hwun Chung Woo Keun Song Soo Hyun Eom Chang-Duk Jun
author_sort	Min-Sung Kwon
title	Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
title_short	Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
title_full	Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
title_fullStr	Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
title_full_unstemmed	Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
title_sort	swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/7351091967914947a9ffcb3ab1133653
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Swiprosin-1 is a novel actin bundling protein that regulates cell spreading and migration.

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