ARF family G proteins and their regulators: roles in membrane transport, development and disease.

ARF family G proteins and their regulators: roles in membrane transport, development and disease.
复制标题

DOI:
10.1038/nrm3117
复制
发表时间:
2011-06
期刊:
Nature reviews. Molecular cell biology
影响因子:
--
通讯作者:
--
中科院分区:
其他
文献类型:
--
作者:

文献摘要

参考文献

被引文献

相似文献

鸟嘌呤核苷酸结合(G)蛋白的adp -核糖基化因子(ARF)家族,包括ARF蛋白、ARF样(ARL)蛋白和SAR1,调节膜交通和细胞器结构,每个家族成员都通过GTP结合和GTP水解的循环进行调节,分别激活和灭活G蛋白。传统上,arf的特点是其在招募外壳蛋白以驱动货物分选、招募可以改变膜脂组成的酶和调节细胞骨架因子方面的直接作用。现在,在高尔基复合体中发现了arf的新作用,例如在驱动脂质运输中。ARL蛋白也越来越多地与细胞骨架过程的贩运协调联系在一起,例如在纤毛发生过程中。人们对控制介导GTP与ARF结合的ARF鸟嘌呤核苷酸交换因子(GEF)募集的机制特别感兴趣,在细胞聚素(也称为ARNO) GEF的情况下,膜募集与自身抑制的缓解相结合。gef如细胞聚丝素也可能参与特定arf对之间的级联激活。传统上,G蛋白信号传导被视为线性途径,与gdp结合形式的ARF蛋白是无活性的;然而,最近的研究强调了这些与gdp结合的形式的新作用,并表明gef和gtpase激活蛋白(gap)本身可以通过支架功能参与不同的信号反应。adp -核糖基化因子(ARF)和ARF样(ARL) G蛋白家族,已知调节膜运输和细胞器结构,正在成为多种过程的调节剂,包括脂质和细胞骨架运输。虽然传统上被视为线性信号通路的一部分,但ARF及其调控因子现在必须被认为存在于功能网络中,其中“非活性”ARF和调控因子本身都可以介导不同的作用。鸟嘌呤核苷酸结合蛋白(G)的adp核糖基化因子(ARF)家族成员,包括ARF样(ARL)蛋白和SAR1,通过招募货物分选外壳蛋白、调节膜脂组成以及与其他G蛋白的调节因子相互作用来调节膜运输和细胞器结构。ARF和ARL蛋白的新作用正在出现,包括在高尔基复合体和纤毛形成中的新功能。它们的功能受严格的空间调控,由分别催化GTP交换和水解的鸟嘌呤核苷酸交换因子(GEFs)和gtpase激活蛋白(GAPs)介导。我们对功能网络的理解正在取得重要进展,这些功能网络不仅是由gef和gap本身形成的,也是由ARF蛋白的非活性形式形成的。
The ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF proteins, ARF-like (ARL) proteins and SAR1, regulates membrane traffic and organelle structure, and each family member is regulated through a cycle of GTP binding and GTP hydrolysis, which activate and inactivate, respectively, the G protein. Traditionally, ARFs have been characterized for their immediate effects in the recruitment of coat proteins to drive cargo sorting, the recruitment of enzymes that can alter membrane lipid composition and the regulation of cytoskeletal factors. Now, new roles for ARFs have been discovered at the Golgi complex, for example in driving lipid transport. ARL proteins are also being increasingly linked to coordination of trafficking with cytoskeletal processes, for example during ciliogenesis. There is particular interest in the mechanisms that control recruitment of the ARF guanine nucleotide exchange factors (GEFs) that mediate GTP binding to ARFs and, in the case of the cytohesin (also known as ARNO) GEF, membrane recruitment is coupled to relief of autoinhibition. GEFs such as cytohesin may also participate in a cascade of activation between particular pairs of ARFs. Traditionally, G protein signalling has been viewed as a linear pathway, with the GDP-bound form of an ARF protein being inactive; however, more recent studies have highlighted novel roles for these GDP-bound forms and have also shown that GEFs and GTPase-activating proteins (GAPs) themselves can engage in distinct signalling responses through scaffolding functions. The ADP-ribosylation factor (ARF) and ARF-like (ARL) family of G proteins, which are known to regulate membrane traffic and organelle structure, are emerging as regulators of diverse processes, including lipid and cytoskeletal transport. Although traditionally viewed as part of a linear signalling pathway, ARFs and their regulators must now be considered to exist within functional networks, in which both the 'inactive' ARF and the regulators themselves can mediate distinct effects. Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G proteins. New roles of ARF and ARL proteins are emerging, including novel functions at the Golgi complex and in cilia formation. Their function is under tight spatial control, which is mediated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) that catalyse GTP exchange and hydrolysis, respectively. Important advances are being gained in our understanding of the functional networks that are formed not only by the GEFs and GAPs themselves but also by the inactive forms of the ARF proteins.
DOI: 10.1371/journal.pbio.0060292
发表时间: 2008-11-25
期刊: PLoS biology
影响因子: 9.8
作者:
Beller M;Sztalryd C;Southall N;Bell M;Jäckle H;Auld DS;Oliver B
通讯作者: Oliver B
DOI: 10.1021/bi962252b
发表时间: 1997-04-15
期刊: BIOCHEMISTRY
影响因子: 2.9
作者:
Antonny, B;BeraudDufour, S;Chabre, M
通讯作者: Chabre, M
DOI: 10.1371/journal.pbio.0040162
发表时间: 2006-06
期刊: PLoS biology
影响因子: 9.8
作者:
Beemiller P;Hoppe AD;Swanson JA
通讯作者: Swanson JA
DOI: 10.1091/mbc.e06-11-0998
发表时间: 2007-06-01
影响因子: 3.3
作者:
Cohen, Lee Ann;Honda, Akira;Donaldson, Julie G.
通讯作者: Donaldson, Julie G.
DOI: 10.1016/j.molcel.2007.09.017
发表时间: 2007-11-30
期刊: MOLECULAR CELL
影响因子: 16
作者:
DiNitto, Jonathan P.;Delprato, Anna;Lambright, David G.
通讯作者: Lambright, David G.