Europe PMC

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our privacy notice and cookie policy.

Clustering of the high affinity Fc receptor for immunoglobulin G (Fc gamma RI) results in phosphorylation of its associated gamma-chain.

Author information

Affiliations

  • 1. Department of Internal Medicine, Ohio State University College of Medicine, Columbus 43210.
      Authors
    • Duchemin AM 1
    (1 author)

The Journal of Biological Chemistry, 01 Apr 1994, 269(16):12111-12117
https://doi.org/10.1016/s0021-9258(17)32688-1 PMID: 7512959 

Abstract 

We are investigating the role of gamma-chain in functions mediated by the high affinity Fc receptor for IgG (Fc gamma RI). In a previous study, we found that gamma-chain, which is a member of the family of zeta-chain proteins, associates with Fc gamma RI. Here we show that clustering of Fc gamma RI leads to a rapid and transient tyrosine phosphorylation of gamma-chain in U937 cells. The response was limited to Fc gamma RI activation, and no phosphorylation of gamma-chain was observed after cross-linking of monoclonal antibodies to other surface receptors on these cells. The gamma-chain phosphorylated after Fc gamma RI clustering was the gamma-chain associated with the receptor. We also identified Syk as one of the kinases associated with the receptor complex. Upon Fc gamma RI activation, Syk, but not ZAP-70, was phosphorylated, and reimmunoadsorption experiments of phosphoproteins from immune complex in vitro kinase assays indicated that Syk is part of the activated gamma-chain-Fc gamma RI complex. These results suggest that gamma-chain links Fc gamma RI to intracellular transduction pathways.

Full text links 

Read article at publisher's site: https://doi.org/10.1016/s0021-9258(17)32688-1

Free to read at intl.jbc.org
http://intl.jbc.org/cgi/content/abstract/269/16/12111

Citations & impact 

Impact metrics

43
Citations
Jump to Citations
11
Data citations
Jump to Data

Citations of article over time

Smart citations by scite.ai
Smart citations by scite.ai include citation statements extracted from the full text of the citing article. The number of the statements may be higher than the number of citations provided by EuropePMC if one paper cites another multiple times or lower if scite has not yet processed some of the citing articles.
Explore citation contexts and check if this article has been supported or disputed.
https://scite.ai/reports/10.1016/s0021-9258(17)32688-1

Supporting
Mentioning
Contrasting
0
14
0

Article citations

Go to all (43) article citations

Data 

Similar Articles 

To arrive at the top five similar articles we use a word-weighted algorithm to compare words from the Title and Abstract of each citation.

Funding 

Funders who supported this work.

NCI NIH HHS (1)