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通过广泛的可变剪接产生的两组结构不同的人类荷马蛋白的分子特征分析。

Molecular characterisation of two structurally distinct groups of human homers, generated by extensive alternative splicing.

作者信息

Soloviev M M, Ciruela F, Chan W Y, McIlhinney R A

机构信息

Medical Research Council Anatomical Neuropharmacology Unit, Mansfield Road, Oxford, OX1 3TH, UK.

出版信息

J Mol Biol. 2000 Feb 4;295(5):1185-200. doi: 10.1006/jmbi.1999.3436.

DOI:10.1006/jmbi.1999.3436
PMID:10653696
Abstract

Homer proteins bind specifically to the C termini of the metabotropic glutamate receptor mGluR1alpha/a and mGluR5, play a role in their targeting and modulate their synaptic properties. We have discovered that extensive alternative splicing generates a family of 17 Homer proteins. These fall into two distinct groups of 12 "long" Homers, which all have a coiled-coil domain at their C termini, and five "short" Homers, which lack such a domain. All Homers contain the N-terminal sequence responsible for their binding to mGluR1alpha/a receptors and can be co-localised with the recombinantly expressed mGluR1alpha/a protein in HEK-293 cells. The existence of the long and the short variants of each of the Homer-1, Homer-2 and Homer-3 proteins reflects the fundamental principles of Homer functions.

摘要

荷马蛋白特异性结合代谢型谷氨酸受体mGluR1α/a和mGluR5的C末端,在其靶向定位中发挥作用并调节其突触特性。我们发现广泛的可变剪接产生了一个由17种荷马蛋白组成的家族。这些蛋白分为两组,一组是12种“长”荷马蛋白,它们在C末端都有一个卷曲螺旋结构域;另一组是5种“短”荷马蛋白,它们缺乏这样的结构域。所有荷马蛋白都含有负责与mGluR1α/a受体结合的N末端序列,并且可以在HEK-293细胞中与重组表达的mGluR1α/a蛋白共定位。荷马-1、荷马-2和荷马-3蛋白各自的长变体和短变体的存在反映了荷马蛋白功能的基本原理。

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J Mol Biol. 2000 Feb 4;295(5):1185-200. doi: 10.1006/jmbi.1999.3436.
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