PMID- 1834946
OWN - NLM
STAT- MEDLINE
DCOM- 19911202
LR  - 20091119
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 353
IP  - 6347
DP  - 1991 Oct 31
TI  - Phosphorylation and dephosphorylation of the high-affinity receptor for 
      immunoglobulin E immediately after receptor engagement and disengagement.
PG  - 855-8
AB  - Triggering of mast cells and basophils by immunoglobulin E (IgE) and antigen 
      induces various biochemical signals, including tyrosine kinase activation, which 
      lead to cell degranulation and the release of mediators of the allergic reaction. 
      The high-affinity receptor for IgE (Fc epsilon RI) responsible for initiating 
      these events is a complex structure composed of an IgE-binding alpha-chain, a 
      beta-chain and a homodimer of gamma-chains. It has been assumed that beta and 
      gamma, which have extensive cytoplasmic domains, play an important but undefined 
      role in coupling Fc epsilon RI to signal transduction mechanisms. Here we show 
      that Fc epsilon RI engagement induces immediate in vivo phosphorylation on beta 
      (tyrosine and serine) and gamma (tyrosine and threonine) by at least two 
      different non-receptor kinases. We take advantage of unique features of this 
      receptor system to demonstrate that the phosphorylation signal is restricted to 
      activated receptors and is immediately reversible upon receptor disengagement by 
      undefined phosphatases. Rapid phosphorylation and dephosphorylation may be a 
      general mechanism to couple and uncouple activated receptors to other effector 
      molecules. This could be particularly relevant to other multimeric receptors 
      containing Fc epsilon RI gamma-chains or the related zeta and eta chains such as 
      the T-cell antigen receptor (TCR) and the low-affinity receptor for 
      immunoglobulin G (Fc gamma RIII, CD16).
FAU - Paolini, R
AU  - Paolini R
AD  - Molecular Allergy and Immunology Section, National Institute of Allergy and 
      Infectious Diseases, National Institutes of Health, Rockville, Maryland 20852.
FAU - Jouvin, M H
AU  - Jouvin MH
FAU - Kinet, J P
AU  - Kinet JP
LA  - eng
PT  - Journal Article
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Phosphoproteins)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
SB  - IM
MH  - Animals
MH  - Antigens, Differentiation, B-Lymphocyte/isolation & purification/*metabolism
MH  - Cell Line
MH  - Cell Membrane/immunology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Immunoglobulin E/*metabolism
MH  - Leukemia, Experimental
MH  - Macromolecular Substances
MH  - Molecular Weight
MH  - Phosphoproteins/isolation & purification
MH  - Phosphorylation
MH  - Protein-Tyrosine Kinases/metabolism
MH  - Rats
MH  - Receptors, Fc/isolation & purification/*metabolism
MH  - Receptors, IgE
EDAT- 1991/10/31 00:00
MHDA- 1991/10/31 00:01
CRDT- 1991/10/31 00:00
PHST- 1991/10/31 00:00 [pubmed]
PHST- 1991/10/31 00:01 [medline]
PHST- 1991/10/31 00:00 [entrez]
AID - 10.1038/353855a0 [doi]
PST - ppublish
SO  - Nature. 1991 Oct 31;353(6347):855-8. doi: 10.1038/353855a0.