JOURNAL ARTICLE
RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
REVIEW
Add like
Add dislike
Add to saved papers

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

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.

Full text links

We have located links that may give you full text access.
Can't access the paper?
Try logging in through your university/institutional subscription. For a smoother one-click institutional access experience, please use our mobile app.

For the best experience, use the Read mobile app

Mobile app image

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app

All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.

By using this service, you agree to our terms of use and privacy policy.

Your Privacy Choices Toggle icon

You can now claim free CME credits for this literature searchClaim now

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app