3D Structure and Interaction of p24β and p24δ Golgi Dynamics Domains: Implication for p24 Complex Formation and Cargo Transport
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- 作者：Masamichi Nagae1 ; Tetsuya Hirata2 ; Kana Morita-Matsumoto1 ; Romina Theiler2 ; 4 ; Morihisa Fujita2 ; 3 ; Taroh Kinoshita2 ; Yoshiki Yamaguchi1 ; yyoshiki@riken.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：TMED ; transmembrane Emp24 protein transport domain ; COP ; coat protein ; ER ; endoplasmic reticulum ; GOLD ; Golgi dynamics ; GPI-AP ; glycosylphosphatidylinositol-anchored protein ; myc-p24δ1 ; myc-tagged p24δ1 ; KO ; knockout ; VFG-GPI ; VSVGts-FLAG-mEGFP-GPI ; Dox ; doxycycline ; SAD ; single anomalous diffraction ; SeMet ; selenomethionine ; HSQC ; heteronuclear single quantum coherence ; Br ; Bromide
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：4087-4099
- 全文大小：1462 K
文摘
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p24 family proteins are involved in intracellular protein transport.
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p24δ1 GOLD domain is essential for efficient transport of glycosylphosphatidylinositol-anchored proteins.
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p24β1 and p24δ1 GOLD domains have a β-sandwich fold with an intrasheet disulfide bridge.
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p24β1 and p24δ1 GOLD domains interact weakly.
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Interaction of GOLD domains may contribute to p24 hetero-oligomeric complex formation.