Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis.
Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis.
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独特的N-末端相互作用将F-BOX应激诱导（FBS）蛋白连接到拟南芥中的WD 40重复样蛋白途径。
DOI：
10.3390/plants10102228
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发表时间：
2021-10-19
期刊：
影响因子：
--
通讯作者：
Thines B
中科院分区：
文献类型：
--
作者：
Sepulveda-Garcia E;Fulton EC;Parlan EV;O'Connor LE;Fleming AA;Replogle AJ;Rocha-Sosa M;Gendron JM;Thines B
SCF型E3泛素连接酶为植物中的许多选择性蛋白质降解事件提供特异性，包括那些能够在环境胁迫下存活的事件。SCF复合物使用F-box（FBX）蛋白作为可互换的底物衔接子，以招募泛素化的蛋白质靶点。FBX蛋白几乎普遍具有具有两个结构域的结构：保守的N-末端F-box结构域与SKP蛋白相互作用并将FBX蛋白连接到核心SCF复合物，而C-末端结构域与蛋白质靶标相互作用并促进募集。F-box应激诱导（FBS）植物FBX蛋白亚家族具有非典型结构，然而，具有位于中心的F-box结构域和在N-和C-末端的额外保守区域。FBS蛋白与环境应激网络有关，但尚未确定该亚家族的泛素化靶点或生物学功能。我们在拟南芥中鉴定了两个WD 40重复序列样蛋白，它们在植物中高度保守，并与FBS蛋白相互作用，我们将其命名为FBS相互作用蛋白（FBIPs）。FBIP仅与FBS蛋白的N-末端相互作用，并且这种相互作用发生在细胞核中。FBS 1使FBIP 1不稳定，这与FBIP是泛素化靶向SCFFBS 1复合物一致。这项工作表明，FBS蛋白可能在应激反应的核事件中发挥作用，它确定了两个WD 40重复样蛋白作为新的工具，以探测如何通过FBX蛋白N-末端相互作用事件的非典型SCF复合物，SCFFBS，功能。
SCF-type E3 ubiquitin ligases provide specificity to numerous selective protein degradation events in plants, including those that enable survival under environmental stress. SCF complexes use F-box (FBX) proteins as interchangeable substrate adaptors to recruit protein targets for ubiquitylation. FBX proteins almost universally have structure with two domains: A conserved N-terminal F-box domain interacts with a SKP protein and connects the FBX protein to the core SCF complex, while a C-terminal domain interacts with the protein target and facilitates recruitment. The F-BOX STRESS INDUCED (FBS) subfamily of plant FBX proteins has an atypical structure, however, with a centrally located F-box domain and additional conserved regions at both the N- and C-termini. FBS proteins have been linked to environmental stress networks, but no ubiquitylation target(s) or biological function has been established for this subfamily. We have identified two WD40 repeat-like proteins in Arabidopsis that are highly conserved in plants and interact with FBS proteins, which we have named FBS INTERACTING PROTEINs (FBIPs). FBIPs interact exclusively with the N-terminus of FBS proteins, and this interaction occurs in the nucleus. FBS1 destabilizes FBIP1, consistent with FBIPs being ubiquitylation targets SCFFBS1 complexes. This work indicates that FBS proteins may function in stress-responsive nuclear events, and it identifies two WD40 repeat-like proteins as new tools with which to probe how an atypical SCF complex, SCFFBS, functions via FBX protein N-terminal interaction events.
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影响因子：
4.4
作者：
Gonzalez LE;Keller K;Chan KX;Gessel MM;Thines BC
通讯作者：
Thines BC
影响因子：
64.8
作者：
Más, P;Kim, WY;Kay, SA
通讯作者：
Kay, SA
DOI：
10.1073/pnas.162339999
发表时间：
2002-08-20
影响因子：
11.1
作者：
Gagne, JM;Downes, BP;Vierstra, RD
通讯作者：
Vierstra, RD
影响因子：
5.6
作者：
Long, Yun;Schiefelbein, John
通讯作者：
Schiefelbein, John
影响因子：
13.6
作者：
Ke J;Ma H;Gu X;Thelen A;Brunzelle JS;Li J;Xu HE;Melcher K
通讯作者：
Melcher K