Molecular cloning of an amphibian insulin receptor substrate 1-like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation
Molecular cloning of an amphibian insulin receptor substrate 1-like cDNA and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus oocyte maturation
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两栖类胰岛素受体底物 1 样 cDNA 的分子克隆以及磷脂酰肌醇 3-激酶参与胰岛素诱导的非洲爪蟾卵母细胞成熟
DOI：
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发表时间：
1995
影响因子：
5.3
通讯作者：
T. Pawson
中科院分区：
文献类型：
--
作者：
X. J. Liu;A. Sorisky;L. Zhu;T. Pawson
以大鼠胰岛素受体底物1（IRS-1）cDNA为探针，通过低严格性杂交，从非洲爪蟾卵巢cDNA文库中分离到一个IRS-1样cDNA。由该cDNA编码的推导的氨基酸序列（称为XIRS-L）与大鼠IRS-1的氨基酸序列有67%相同（77%相似）。值得注意的是，在大鼠IRS-1中鉴定的所有胰岛素诱导的酪氨酸磷酸化位点，包括负责与磷脂酰肌醇（PI）3-激酶的Src同源结构域、Syp和Grb 2结合的位点，在XIRS-L中是保守的。在非洲爪蟾未成熟卵母细胞中可检测到相应于克隆的XIRS-L的mRNA和蛋白。在昆虫细胞中产生的重组XIRS-L蛋白或含有推定的PI 3-激酶结合位点的细菌谷胱甘肽S-转移酶融合蛋白可以在体外被纯化的胰岛素受体激酶（IRK）结构域磷酸化，并且IRK催化的磷酸化使得这两种蛋白能够结合爪蟾卵母细胞裂解物中的PI 3-激酶。另一个谷胱甘肽S-转移酶融合蛋白含有XIRS-L的C末端，并包括几个推定的酪氨酸磷酸化位点，也被IRK在体外磷酸化，但它不能结合PI 3-激酶。胰岛素刺激未成熟非洲爪蟾卵母细胞激活体内PI 3-激酶[如PI（3，4）P2和PI（3，4，5）P3升高所示]以及卵母细胞成熟（如生殖囊泡破裂所示）。这些卵母细胞与渥曼青霉素预处理抑制胰岛素诱导的PI 3-激酶在体内的激活。同样的处理也消除了胰岛素诱导的，但不是孕酮诱导的，germinal囊泡破裂。这些结果（i）确定IRS-1样分子在未成熟的非洲爪蟾卵母细胞，表明IRS-1样Scr同源2结构域对接蛋白在信号转导中的使用是保守的脊椎动物，和（ii）强烈暗示PI 3-激酶作为胰岛素诱导的卵母细胞成熟的重要效应。
An insulin receptor substrate 1 (IRS-1)-like cDNA was isolated from a Xenopus ovary cDNA library by low-stringency hybridization using rat IRS-1 cDNA as a probe. The deduced amino acid sequence encoded by this cDNA (termed XIRS-L) is 67% identical (77% similar) to that of rat IRS-1. Significantly, all the insulin-induced tyrosine phosphorylation sites identified in rat IRS-1, including those responsible for binding to the Src homology domains of phosphatidylinositol (PI) 3-kinase, Syp and Grb2, are conserved in XIRS-L. Both mRNA and protein corresponding to the cloned XIRS-L can be detected in immature Xenopus oocytes. Recombinant XIRS-L protein produced in insect cells or a bacterial glutathione S-transferase fusion protein containing the putative PI 3-kinase binding site can be phosphorylated in vitro by purified insulin receptor kinase (IRK) domain, and the IRK-catalyzed phosphorylation renders both proteins capable of binding PI 3-kinase in Xenopus oocyte lysates. Another glutathione S-transferase fusion protein containing the C terminus of XIRS-L and including several putative tyrosine phosphorylation sites is also phosphorylated by IRK in vitro, but it failed to bind PI 3-kinase. Insulin stimulation of immature Xenopus oocytes activates PI 3-kinase in vivo [as indicated by an elevation of PI(3,4)P2 and PI(3,4,5)P3] as well as oocyte maturation (as indicated by germinal vesicle breakdown). Pretreatment of these oocytes with wortmannin inhibited insulin-induced activation of PI 3-kinase in vivo. The same treatment also abolished insulin-induced, but not progesterone-induced, germinal vesicle breakdown. These results (i) identify an IRS-1-like molecule in immature Xenopus oocytes, suggesting that the use of IRS-1-like Scr homology 2 domain-docking proteins in signal transduction is conserved in vertebrates, and (ii) strongly implicate PI 3-kinase as an essential effector of insulin-induced oocyte maturation.
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影响因子：
4.8
作者：
M. G. Myers;X. Sun;B. Cheatham;BOZENA R. Jachna;Erin Glasheen;J. Backer;M. White
通讯作者：
M. G. Myers;X. Sun;B. Cheatham;BOZENA R. Jachna;Erin Glasheen;J. Backer;M. White
影响因子：
2.9
作者：
GUAN, KL;DIXON, JE
通讯作者：
DIXON, JE
DOI：
10.1073/pnas.89.3.1123
发表时间：
1992-02-01
影响因子：
11.1
作者：
PLUTZKY, J;NEEL, BG;ROSENBERG, RD
通讯作者：
ROSENBERG, RD
胰岛素受体底物 1 与含有 SH2 的磷酸酪氨酸磷酸酶 Syp 结合。
DOI：
--
发表时间：
1993
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Kuhné,MR;Pawson,T;Lienhard,GE;Feng,GS
通讯作者：
Feng,GS
小鼠脂肪细胞中胰岛素诱导的 160 kDa 磷酸酪氨酸蛋白是胰岛素受体底物 1：通过克隆鉴定。
DOI：
10.1016/0167-4781(93)90222-y
发表时间：
1993
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
Keller,SR;Aebersold,R;Garner,CW;Lienhard,GE
通讯作者：
Lienhard,GE