桩蛋白家族成员函数作为Csk-binding蛋白质调节林恩活动在人类和小鼠血小板。
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拉索尔教授VB,冈田克也M,纽曼PJ,纽曼DK
桩蛋白家族成员函数作为Csk-binding蛋白质调节林恩活动在人类和小鼠血小板。
j . 2007 4月15日,403 (2):275 - 81。
- PubMed ID
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17233630 (在PubMed]
- 文摘
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SFKs (Src家族激酶)重要的是有助于止血法血小板功能。SFK活动是由埋头(c端Src激酶)的磷酸化SFKs c端酪氨酸残基,导致抑制SFK活动。埋头SFK活动招募网站由酪氨酸磷酸化Csk-binding蛋白质。桩蛋白,多畴的适配器蛋白质,已经被证明可以作为Csk-binding蛋白质和抑制Src在生长因子信号活动。人类血小板表达Hic-5桩蛋白家族的一个成员;然而,它能够充当Csk-binding蛋白质没有特点。我们试图识别和描述桩蛋白能力的家庭成员作为Csk-binding蛋白质在血小板激活。我们发现,小鼠和人类血小板不同的补桩蛋白家族成员表达。人类血小板表达Hic-5,而小鼠血小板表达桩蛋白和leupaxin除了Hic-5。在人类血小板聚集,Hic-5酪氨酸磷酸化和招募埋头通过SH2域。 In aggregating murine platelets, however, Csk bound preferentially to paxillin, even though both paxillin and Hic-5 were abundantly present and became tyrosine phosphorylated. The SFK Lyn, but not Src or Fyn, was associated with paxillin family members in resting and aggregated human and murine platelets. Lyn, however, was phosphorylated on its C-terminal inhibitory tyrosine residue only following platelet aggregation, which was coincident with recruitment of Csk to paxillin and/or Hic-5 in a manner dependent on prior alpha(IIb)beta3 engagement. These observations support the notion that Hic-5 and paxillin function as negative feedback regulators of SFKs in aggregated platelets and that, when both are present, paxillin is preferentially used.