The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.

The structure of the Myo4p globular tail and its function in ASH1 mRNA localization.
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DOI:
10.1083/jcb.201002076
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发表时间:
2010-05-03
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Niessing D
Niessing D
中科院分区:
其他
文献类型:
--
作者:
Heuck A;Fetka I;Brewer DN;Hüls D;Munson M;Jansen RP;Niessing D

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V型肌球蛋白球状尾部的保守氨基酸补丁结合She 3 p将ASH 1 mRNA定位于分裂的酵母细胞的芽中。V型肌球蛋白(MyoV)依赖的货物运输是真核生物中的一个重要过程。对酵母和脊椎动物MyoV的研究表明,它们的球状尾巴介导与货物复合物的结合。在酿酒酵母中,MyoV马达Myo 4p与She 3 p相互作用以将HO 1(ASH 1)mRNA的不对称合成定位到分裂细胞的芽中。最近的一项研究表明,GFP-MS 2拴系的ASH 1颗粒的定位不需要Myo 4p球状尾,挑战了该结构域的假定作用。我们更直接地评估了ASH 1 mRNA和Myo 4p的分布,发现它们的定位在表达球状尾缺乏Myo 4p的细胞中受损。体外研究进一步表明,球状尾与更多的N-末端接头区一起是有效的She 3 p结合所需的。我们还确定了Myo 4p球状尾的X射线结构,并确定了一个保守的表面补丁重要的She 3 p结合。该结构显示出明显的相似性,膜拴系复合物,并表明Myo 4p可能不会经历其运动域的自抑制。
A conserved patch of amino acids in the globular tail of type V myosin binds She3p to localize ASH1 mRNA to the bud of dividing yeast cells. Type V myosin (MyoV)–dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2–tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail–lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain.
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