Holowka D, Baird B
Department of Chemistry, Cornell University, Ithaca, New York 14853-1301, USA.
Annu Rev Biophys Biomol Struct. 1996;25:79-112. doi: 10.1146/annurev.bb.25.060196.000455.
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.
免疫球蛋白E的高亲和力受体FcεRI，是介导细胞对外源抗原作出反应并激活的多亚基免疫受体的原型。该受体在肥大细胞和嗜碱性粒细胞表面的抗原介导聚集引发了一个生化级联反应，在这个信号转导过程的最初步骤中，非受体酪氨酸激酶是关键参与者。用结构和价态明确的配体对FcεRI进行交联，揭示了有关功能活性受体聚集体基本要求的详细信息。已通过生化和生物物理方法对这些受体与其他细胞成分相互作用中交联依赖性变化进行了表征，以更全面地了解信号起始过程。最近的证据表明，这一过程涉及聚集的FcεRI与特殊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，但它们为质膜结构和动力学提供了新的见解，这些见解通常与大多数有核哺乳动物细胞的功能相关。
