Dally-like protein, a new Drosophila glypican with expression overlapping with wingless
Dally-like protein, a new Drosophila glypican with expression overlapping with wingless
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Dally 样蛋白，一种新的果蝇磷脂酰肌醇蛋白，其表达与 wingless 重叠
DOI：
10.1016/s0925-4773(00)00502-5
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发表时间：
2000
影响因子：
2.6
通讯作者：
S. Baumgartner
中科院分区：
文献类型：
--
作者：
Narmada A. Khare;S. Baumgartner
蛋白聚糖是细胞外基质的分子，由于其糖胺聚糖（GAG）链和大体积而携带高度负电荷。在发现它们的糖链在成纤维细胞生长因子（FGF）信号传导中的重要性之前，它们被认为在细胞分裂、粘附、血液凝固等活动中起次要作用（Science 252（1991）1705; Cell 64（1991）841）。对无糖（sgl）和无硫酸盐（sfl）基因突变的研究已经证明，参与Wg信号传导的蛋白聚糖含有硫酸乙酰肝素GAG链（Development 124（1997）2623; Development 124（1997）3055; Development 124（1997）3565; Development 126（1999）3715）。这导致了这些分子的特定功能的归属（J. Cell Biol.148（2000）227）。硫酸乙酰肝素蛋白聚糖（HSPG）的磷脂酰肌醇蛋白聚糖家族的特征在于具有保守的半胱氨酸残基的核心蛋白，并且通过糖基磷脂酰肌醇（GPI）锚附着到细胞表面。这可能导致不同于其他HSPG的内吞途径、更高的侧向移动性和细胞中可能的顶端定位（Proc.Natl.Acad.Sci. Acad. Sci，USA 85（1988）9557）。其HS含量的变化可影响结合性质和定位（J. Cell Biol.124（1994）149; J. Cell Biol.132（1996）487），从而使每个成员专门化以实现独特的生物学功能。磷脂酰肌醇蛋白聚糖在形态发生途径中起重要作用，例如人磷脂酰肌醇蛋白聚糖3（GPC 3）在Eschloson-Golabi-Behmel综合征中突变，使个体易于患肿瘤（Nat.Genet. 12（1996）241）。Dally是该家族的第一个果蝇成员，对无翅和十肢瘫痪信号通路至关重要（Development 121（1995）3687; Development 124（1997）4113）。在这里，我们报告了一个新的果蝇磷脂酰肌醇蛋白聚糖，dally-like蛋白（dlp）与磷脂酰肌醇蛋白聚糖的所有功能。基于表达研究，我们报告其与Wg的共定位。
Proteoglycans, the molecules of extracellular matrix, carry a highly negative charge due to their glycosaminoglycan (GAG) chains and large volumes. They were considered to play a secondary role in activities like cell division, adhesion, blood coagulation, etc. until the importance of their sugar chains in the fibroblast growth factor (FGF) signalling was discovered (Science 252 (1991) 1705; Cell 64 (1991) 841). Studies of mutations in the genes sugarless(sgl) and sulfateless (sfl) have proved that the proteoglycans involved in Wg signalling contain heparan sulfate GAG chains (Development 124 (1997) 2623; Development 124 (1997) 3055; Development 124 (1997) 3565; Development 126 (1999) 3715). This has led to the attribution of specific functions to these molecules (J. Cell Biol. 148 (2000) 227). The Glypican family of heparan sulfate proteoglycans (HSPGs) is characterized by core proteins with conserved cysteine residues and attachment to the cell surface by a glycosylphosphatidyl inositol (GPI) anchor. This may lead to endocytic pathways that are different from other HSPGs, higher lateral mobility and possible apical localisation in a cell (Proc. Natl. Acad. Sci, USA 85 (1988) 9557). Variations in their HS contents may effect binding properties and localisation (J. Cell Biol. 124 (1994) 149; J. Cell Biol. 132 (1996) 487), thus specialising each member for a unique biological function. Glypicans play important roles in morphogenetic pathways, e.g. human glypican 3 (GPC3) is mutated in Simpson-Golabi-Behmel syndrome making an individual prone to tumours (Nat. Genet. 12 (1996) 241). Dally, the first Drosophila member of the family, is essential for the wingless and decapentaplegic signalling pathways (Development 121 (1995) 3687; Development 124 (1997) 4113). Here, we report a new Drosophila glypican, dally-like protein (dlp) with all the features of a glypican. Based on expression studies we report its colocalisation with Wg.