SR proteins and galectins: what's in a name?
SR proteins and galectins: what's in a name?
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DOI：
10.1093/glycob/cwq097
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发表时间：
2010-10
期刊：
影响因子：
4.3
通讯作者：
Wang JL
中科院分区：
文献类型：
--
作者：
Haudek KC;Patterson RJ;Wang JL
虽然富含丝氨酸(S)和精氨酸(R)的剪接因子家族（SR蛋白）的成员最初是根据其在细胞核中的剪接活性纯化的，但最近的文献表明，它们在细胞表面表现出碳水化合物结合活性。相比之下，凝集素是根据其糖结合活性和细胞表面定位分离出来的。然而，令人惊讶的是，可以发现两个成员（半乳糖凝集素-1和半乳糖凝集素-3）与核核糖核蛋白复合物（包括剪接体）相关，并且通过无细胞测定，已被证明是必需的剪接因子。因此，尽管它们最初的兴趣点有所不同，但现在看来，这两个蛋白质家族的成员具有四个关键特性：(a)核和细胞质分布；(b) mrna前剪接活性；(c)碳水化合物结合活性；(d)特定细胞的细胞表面定位。这些发现引发了关于细胞核剪接因子与细胞表面碳水化合物结合蛋白之间关系的令人兴奋的问题。
Although members of the serine (S)- and arginine (R)-rich splicing factor family (SR proteins) were initially purified on the basis of their splicing activity in the nucleus, there is recent documentation that they exhibit carbohydrate-binding activity at the cell surface. In contrast, galectins were isolated on the basis of their saccharide-binding activity and cell surface localization. Surprisingly, however, two members (galectin-1 and galectin-3) can be found in association with nuclear ribonucleoprotein complexes including the spliceosome and, using a cell-free assay, have been shown to be required splicing factors. Thus, despite the difference in terms of their original points of interest, it now appears that members of the two protein families share four key properties: (a) nuclear and cytoplasmic distribution; (b) pre-mRNA splicing activity; (c) carbohydrate-binding activity; and (d) cell surface localization in specific cells. These findings provoke stimulating questions regarding the relationship between splicing factors in the nucleus and carbohydrate-binding proteins at the cell surface.
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