Phosphoproteomes of Strongylocentrotus purpuratus shell and tooth matrix: identification of a major acidic sea urchin tooth phosphoprotein, phosphodontin
Phosphoproteomes of Strongylocentrotus purpuratus shell and tooth matrix: identification of a major acidic sea urchin tooth phosphoprotein, phosphodontin
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DOI：
10.1186/1477-5956-8-6
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发表时间：
2010-02-08
期刊：
影响因子：
2
通讯作者：
Mann, Matthias
中科院分区：
文献类型：
--
作者：
Mann, Karlheinz;Poustka, Albert J.;Mann, Matthias
背景：海胆是发育生物学和生物矿化研究的主要模式生物。然而，识别蛋白质参与幼虫骨骼形成和矿化过程中的胚胎和成人，和这样的蛋白质的分子特征，刚刚获得势头与的Strongylocentrotus purpuratus基因组测序和引入高通量蛋白质组学到field.Results：本报告包含测试（壳）和牙齿有机基质磷酸化蛋白质组的测定。在生物矿物有机基质中共鉴定出34种磷蛋白。大多数磷蛋白是特定的一个隔室，只有两个被确定在两个矩阵。海胆磷酸化蛋白质组含有几种明显的哺乳动物蛋白质的直系同源物，如Src家族酪氨酸激酶、蛋白激酶C-δ 1、Dickkopf-1和其他信号转导成分或核结合蛋白。在大多数情况下，海胆和哺乳动物蛋白质之间的磷酸化位点是保守的。然而，大多数磷蛋白没有哺乳动物的对应物。从生物矿化研究的角度来看，最有趣的海胆特异性磷蛋白是一种丰富的高度磷酸化和非常酸性的牙齿基质蛋白，由35个非常相似的短序列重复序列、一个预测的N-末端分泌信号序列和一个富含Asp-rich的C-末端基序组成，包含在[Glean 3：18919]中。确定的64个磷酸化位点代表了目前实验确定的海胆蛋白磷酸化位点的最全面的列表，并且是最近分析的Strongylocentrotus purpuratus外壳和牙齿蛋白质组的重要补充。鉴定的磷蛋白包括一种主要的高度磷酸化的蛋白质[Glean 3：18919]，我们建议将其命名为phosphodontin。尽管与磷酸化酸性哺乳动物牙齿磷蛋白（phosphoryn）或牙本质基质蛋白-1（dentin matrix protein-1）等高度磷酸化的酸性磷酸化蛋白序列无关，但磷酸化牙本质蛋白在海胆牙齿中可能具有类似的功能。超过一半的检测到的蛋白质以前没有在蛋白质水平上鉴定过，从而证实了以前只被称为基因组序列的蛋白质的存在。
Background: Sea urchin is a major model organism for developmental biology and biomineralization research. However, identification of proteins involved in larval skeleton formation and mineralization processes in the embryo and adult, and the molecular characterization of such proteins, has just gained momentum with the sequencing of the Strongylocentrotus purpuratus genome and the introduction of high-throughput proteomics into the field.Results: The present report contains the determination of test (shell) and tooth organic matrix phosphoproteomes. Altogether 34 phosphoproteins were identified in the biomineral organic matrices. Most phosphoproteins were specific for one compartment, only two were identified in both matrices. The sea urchin phosphoproteomes contained several obvious orthologs of mammalian proteins, such as a Src family tyrosine kinase, protein kinase C-delta 1, Dickkopf-1 and other signal transduction components, or nucleobindin. In most cases phosphorylation sites were conserved between sea urchin and mammalian proteins. However, the majority of phosphoproteins had no mammalian counterpart. The most interesting of the sea urchin-specific phosphoproteins, from the perspective of biomineralization research, was an abundant highly phosphorylated and very acidic tooth matrix protein composed of 35 very similar short sequence repeats, a predicted N-terminal secretion signal sequence, and an Asp-rich C-terminal motif, contained in [Glean3:18919].Conclusions: The 64 phosphorylation sites determined represent the most comprehensive list of experimentally identified sea urchin protein phosphorylation sites at present and are an important addition to the recently analyzed Strongylocentrotus purpuratus shell and tooth proteomes. The identified phosphoproteins included a major, highly phosphorylated protein, [Glean3:18919], for which we suggest the name phosphodontin. Although not sequence-related to such highly phosphorylated acidic mammalian dental phosphoproteins as phosphoryn or dentin matrix protein-1, phosphodontin may perform similar functions in the sea urchin tooth. More than half of the detected proteins were not previously identified at the protein level, thus confirming the existence of proteins only known as genomic sequences previously.