IDENTIFICATION OF 4 MURINE CDNAS ENCODING PUTATIVE PROTEIN-KINASES FROM PRIMITIVE EMBRYONIC STEM-CELLS DIFFERENTIATED IN-VITRO
IDENTIFICATION OF 4 MURINE CDNAS ENCODING PUTATIVE PROTEIN-KINASES FROM PRIMITIVE EMBRYONIC STEM-CELLS DIFFERENTIATED IN-VITRO
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DOI：
10.1073/pnas.90.15.7044
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发表时间：
1993-08-01
影响因子：
11.1
通讯作者：
EMERSON, SG
中科院分区：
文献类型：
--
作者：
BIESECKER, LG;GOTTSCHALK, LR;EMERSON, SG
蛋白激酶通过酪氨酸、丝氨酸或苏氨酸残基的直接磷酸化从造血系统和其它系统中的细胞外配体传递信号。对于在发育的最早阶段很重要的配体和受体知之甚少，干细胞自我更新和谱系定型。我们利用小鼠胚胎干细胞系统的谱系分化潜能克隆了编码四种假定蛋白激酶的部分cDNA。四个基因中的三个在蛋白激酶家族的结构域VII中含有高度保守的残基Asp-Phe-Gly。这些基因是调节胚胎发生中自我更新和谱系定型的细胞因子的受体或下游效应子的候选者。
Protein kinases transduce signals from extracellular ligands in the hematopoietic and other systems through direct phosphorylation of tyrosine, serine, or threonine residues. Little is known about the ligands and receptors that are important in the earliest stages of development-i.e., stem cell self-renewal and lineage commitment. We have made use of the lineage differentiation potential of the murine embryonic stem cell system to clone partial cDNAs encoding four putative protein kinases. Three of the four genes contain the highly conserved residues Asp-Phe-Gly in domain VII of the protein kinase family. These genes are candidates for receptors or downstream effectors of cytokines that regulate self-renewal and lineage commitment in embryogenesis.