Antigen-mediated IGE receptor aggregation and signaling: a window on cell surface structure and dynamics.

Antigen-mediated IGE receptor aggregation and signaling: a window on cell surface structure and dynamics.
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抗原介导的 IGE 受体聚集和信号传导:细胞表面结构和动力学的窗口。

DOI:
10.1146/annurev.bb.25.060196.000455
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发表时间:
1996
期刊:
Annual review of biophysics and biomolecular structure
影响因子:
--
通讯作者:
Baird,B
Baird,B
中科院分区:
--
文献类型:
--
作者:
Holowka,D;Baird,B

文献摘要

被引文献

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免疫球蛋白E的高亲和力受体Fc epsilon RI作为多亚单位免疫受体的原型,介导细胞对外来抗原的激活。该受体在肥大细胞和嗜碱性细胞表面的抗原介导聚集启动了一个生化级联反应,该反应使用非受体酪氨酸激酶作为信号转导过程早期步骤的关键参与者。Fc - epsilon RI与结构和价明确的配体的交联揭示了功能活性受体聚集体基本要求的详细信息。这些受体与其他细胞成分相互作用的交联依赖性变化已经用生化和生物物理方法进行了表征,以建立更完整的信号起始视图。最近的证据表明,这一过程涉及到聚集的Fc epsilon RI与特定的质膜结构域的相互作用,这些结构域可能将重要的信号分子定位在聚集的受体附近。尽管这些不同的研究旨在了解一种细胞表面受体的运作,但它们为研究与大多数有核哺乳动物细胞功能相关的质膜结构和动力学提供了新的见解。
The high-affinity receptor for immunoglobulin E, Fc epsilon RI, serves as an archtype for multisubunit immunoreceptors that mediate cell activation in response to foreign antigens. Antigen-mediated aggregation of this receptor at the surface of mast cells and basophils initiates a biochemical cascade that uses nonreceptor tyrosine kinases as key participants in the earliest steps of this signal transduction process. Cross-linking of Fc epsilon RI with ligands of well-defined structure and valency has revealed detailed information about the fundamental requirements for functionally active receptor aggregates. Cross-linking-dependent changes in the interaction of these receptors with other cellular components have been characterized with biochemical and biophysical methods to develop a more complete view of signal initiation. Recent evidence suggests that this process involves the interaction of aggregated Fc epsilon RI with specialized plasma membrane domains that may localize important signaling molecules in the vicinity of aggregated receptors. Although these various studies were aimed toward understanding the operation of one cell surface receptor, they provide new insights into plasma membrane structure and dynamics that are generally relevant to the function of most nucleated mammalian cells.