65 61

Cited 1 times in

TAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions

DC FieldValueLanguage
dc.contributor.author현영민-
dc.date.accessioned2018-08-28T17:18:58Z-
dc.date.available2018-08-28T17:18:58Z-
dc.date.issued2018-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/162475-
dc.description.abstractTAGLN is an actin-binding protein family that comprises three isoforms with theorized roles in smooth muscle differentiation, tumour development, lymphocyte activation, and brain chemistry. However, their fundamental characteristics in regulation of the actin-based cytoskeleton are not fully understood. Here we show that TAGLN2 (including TAGLN1 and TAGLN3) extensively nucleates G-actin polymerization under low-salt conditions, where polymerization would be completely suppressed. The calponin homology domain and actin-binding loop are essential to mechanically connect two adjacent G-actins, thereby mediating multimeric interactions. However, TAGLN2 blocked the Arp2/3 complex binding to actin filaments under physiological salt conditions, thereby inhibiting branched actin nucleation. In HeLa and T cells, TAGLN2 enhanced filopodium-like membrane protrusion. Collectively, the dual functional nature of TAGLN2-G-actin polymerization and Arp2/3 complex inhibition-may account for the mechanisms of filopodia development at the edge of Arp2/3-rich lamellipodia in various cell types.-
dc.description.statementOfResponsibilityopen-
dc.languageEnglish-
dc.publisherNature Publishing Group-
dc.relation.isPartOfScientific Reports-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleTAGLN2 polymerizes G-actin in a low ionic state but blocks Arp2/3-nucleated actin branching in physiological conditions-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine-
dc.contributor.departmentDept. of Anatomy-
dc.contributor.googleauthorHye-Ran Kim-
dc.contributor.googleauthorMin-Sung Kwon-
dc.contributor.googleauthorSangmin Lee-
dc.contributor.googleauthorYeVin Mun-
dc.contributor.googleauthorKyung-Sik Lee-
dc.contributor.googleauthorChang-Hyun Kim-
dc.contributor.googleauthorBo-Ra Na-
dc.contributor.googleauthorBit Na Rae Kim-
dc.contributor.googleauthorIndre Piragyte-
dc.contributor.googleauthorHyun-Su Lee-
dc.contributor.googleauthorYoungsoo Jun-
dc.contributor.googleauthorMi Sun Jin-
dc.contributor.googleauthorYoung-Min Hyun-
dc.contributor.googleauthorHyun Suk Jung-
dc.contributor.googleauthorJi Young Mun-
dc.contributor.googleauthorChang-Duk Jun-
dc.identifier.doi10.1038/s41598-018-23816-2-
dc.contributor.localIdA04814-
dc.relation.journalcodeJ02646-
dc.identifier.eissn2045-2322-
dc.identifier.pmid29615809-
dc.contributor.alternativeNameHyun, Young-Min-
dc.contributor.affiliatedAuthorHyun, Young-Min-
dc.citation.volume8-
dc.citation.number1-
dc.citation.startPage5503-
dc.identifier.bibliographicCitationScientific Reports, Vol.8(1) : 5503, 2018-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Anatomy (해부학교실) > 1. Journal Papers

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.