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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

Septin Interferes with the Temperature-Dependent Domain Formation and Disappearance of Lipid Bilayer Membranes

http://hdl.handle.net/2237/25714
http://hdl.handle.net/2237/25714
efc086ca-2bdf-47c2-83a6-7a54ef781175
名前 / ファイル ライセンス アクション
la-2016-03452g_R1.pdf la-2016-03452g_R1.pdf ファイル公開:2017/11/15 (3.4 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-03-15
タイトル
タイトル Septin Interferes with the Temperature-Dependent Domain Formation and Disappearance of Lipid Bilayer Membranes
言語 en
著者 Yamada, Shunsuke

× Yamada, Shunsuke

WEKO 69824

en Yamada, Shunsuke

Search repository
Isogai, Takumi

× Isogai, Takumi

WEKO 69825

en Isogai, Takumi

Search repository
Tero, Ryugo

× Tero, Ryugo

WEKO 69826

en Tero, Ryugo

Search repository
Tanaka-Takiguchi, Yohko

× Tanaka-Takiguchi, Yohko

WEKO 69827

en Tanaka-Takiguchi, Yohko

Search repository
Ujihara, Toru

× Ujihara, Toru

WEKO 69828

en Ujihara, Toru

Search repository
Kinoshita, Makoto

× Kinoshita, Makoto

WEKO 69829

en Kinoshita, Makoto

Search repository
Takiguchi, Kingo

× Takiguchi, Kingo

WEKO 69830

en Takiguchi, Kingo

Search repository
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利
言語 en
権利情報 “This document is the Accepted Manuscript version of a Published Work that appeared in final form in [Langmuir], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [http://pubsdc3.acs.org/articlesonrequest/AOR-pbvPuXFPRVfFBTfBYsVj].”
抄録
内容記述 Domain formation or compartmentalization in a lipid bilayer membrane has been thought to take place dynamically in cell membranes and play important roles in the spatiotemporal regulation of their physiological functions. In addition, the membrane skeleton, which is a protein assembly beneath the cell membrane, also regulates the properties as well as the morphology of membranes because of its role as a diffusion barrier against constitutive molecules of the membrane or as a scaffold for physiological reactions. Therefore, it is important to study the relationship between lipid bilayer membranes and proteins that form the membrane skeleton. Among cytoskeletal systems, septin is unique because it forms arrays on liposomes that contain phosphoinositides, and this property is thought to contribute to the formation of the annulus in sperm flagellum. In this study, a supported lipid bilayer (SLB) was used to investigate the effect of septin on lipid bilayers because SLBs rather than liposomes are suitable for observation of the membrane domains formed. We found that SLBs containing phosphatidylinositol (PI) reversibly form domains by decreasing the temperature and that septin affects both the formation and the disappearance of the cooling-induced domain. Septin inhibits the growth of cooling-induced domains during decreases in temperature and inhibits the dispersion and the disappearance of those domains during increases in temperature. These results indicate that septin complexes, i.e., filaments or oligomers assembling on the surface of lipid bilayer membranes, can regulate the dynamics of domain formation via their behavior as an anchor for PI molecules.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 ACS Publications
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1021/acs.langmuir.6b03452
ISSN
収録物識別子タイプ PISSN
収録物識別子 0743-7463
書誌情報 en : Langmuir

巻 32, 号 48, p. 12823-12832, 発行日 2016-11-15
著者版フラグ
値 author
URI
識別子 http://doi.org/10.1021/acs.langmuir.6b03452
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/25714
識別子タイプ HDL
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