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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Class ⅠA phosphoinositide 3-kinases are obligate p85-p110 heterodimers
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Class ⅠA phosphoinositide 3-kinases are obligate p85-p110 heterodimers

机译：ⅠA类磷酸肌醇3-激酶是专性的p85-p110异二聚体

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摘要

Class ⅠA phosphoinositide 3-kinases (PI3Ks) signal downstream of tyrosine kinases and Ras and control a wide variety of biological responses. In mammals, these heterodimeric PI3Ks consist of a p110 catalytic subunit (p110α, p110β, or p110δ) bound to any of five distinct regulatory subunits (p85α, p85β, p55γ, p55α, and p50α, collectively referred to as "p85s"). The relative expression levels of p85 and p110 have been invoked to explain key features of PI3K signaling. For example, free (i.e., non-p110-bound) p85α has been proposed to negatively regulate PI3K signaling by competition with p85/p110 for recruitment to phosphotyrosine docking sites. Using affinity and ion exchange chromatography and quantitative mass spectrometry, we demonstrate that the p85 and p110 subunits are present in equimolar amounts in mammalian cell lines and tissues. No evidence for free p85 or p110 subunits could be obtained. Cell lines contain 10,000-15,000 p85/p110 complexes per cell, with p110β and p110δ being the most prevalent catalytic subunits in nonleukocytes and leukocytes, respectively. These results argue against a role of free p85 in PI3K signaling and provide insights into the nonredundant functions of the different class ⅠA PI3K isoforms.
机译：ⅠA类磷酸肌醇3激酶（PI3K）在酪氨酸激酶和Ras下游发出信号，并控制多种生物学反应。在哺乳动物中，这些异二聚体PI3K由结合至五个不同调节亚基（p85α，p85β，p55γ，p55α和p50α中的任何一个）的p110催化亚基（p110α，p110β或p110δ）组成，统称为“ p85s”。已调用p85和p110的相对表达水平来解释PI3K信号传导的关键特征。例如，已经提出游离的（即，未结合p110的）p85α通过与p85 / p110竞争竞争募集磷酸酪氨酸停靠位点而负调控PI3K信号传导。使用亲和力和离子交换色谱法和定量质谱法，我们证明p85和p110亚基在哺乳动物细胞系和组织中以等摩尔量存在。没有获得免费的p85或p110亚基的证据。细胞系每个细胞包含10,000-15,000个p85 / p110复合物，其中p110β和p110δ分别是非白细胞和白细胞中最普遍的催化亚基。这些结果证明了游离p85在PI3K信号传导中的作用，并提供了对不同的ⅠA类PI3K同工型的非冗余功能的见解。

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