PMID- 24023253
OWN - NLM
STAT- MEDLINE
DCOM- 20140414
LR  - 20211203
IS  - 1937-9145 (Electronic)
IS  - 1945-0877 (Linking)
VI  - 6
IP  - 292
DP  - 2013 Sep 10
TI  - A role for prohibitin in mast cell activation: location matters.
PG  - pe29
LID - 10.1126/scisignal.2004646 [doi]
AB  - Prohibitin 1 (PHB1) and PHB2 are evolutionarily conserved, ubiquitously 
      expressed, pleotropic proteins that control various fundamental cellular 
      processes, including proliferation, migration, metabolism, and death. Studies 
      have unveiled a crucial role for plasma membrane-associated PHBs in regulating 
      tumor metastasis, viral entry, and immune cell activation. A study now identifies 
      a role for PHB1 in the activation of mast cells and allergic reactions mediated 
      by immunoglobulin E (IgE). PHB1 was primarily localized in mast cell granules; 
      however, in response to stimulation with antigen, PHB1 translocated to plasma 
      membrane lipid rafts to form a ternary complex with the high-affinity IgE 
      receptor FcepsilonRIgamma and the nonreceptor tyrosine kinase Syk. Syk became activated, 
      which led to the activation of downstream signaling that stimulated mast cell 
      degranulation and the secretion of cytokines. PHB1 was phosphorylated by the Src 
      family tyrosine kinase Lyn, and palmitoylation of PHB1 was required for its 
      association with the plasma membrane. These observations unveil a previously 
      uncharacterized facet of prohibitin biology and shed further light on the 
      proximal events that drive the activation of FcepsilonRI by IgE in mast cells during 
      allergic reactions.
FAU - Yurugi, Hajime
AU  - Yurugi H
AD  - 1Department of Molecular Biosciences, Faculty of Life Sciences, Kyoto Sangyo 
      University, Kamigamo-Motoyama, Kitaku, Kyoto 603-8555, Japan.
FAU - Rajalingam, Krishnaraj
AU  - Rajalingam K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130910
PL  - United States
TA  - Sci Signal
JT  - Science signaling
JID - 101465400
RN  - 0 (Antigens)
RN  - 0 (FcepsilonRI gamma-chain, human)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (PHB protein, human)
RN  - 0 (PHB2 protein, human)
RN  - 0 (Prohibitins)
RN  - 0 (Receptors, IgE)
RN  - 0 (Repressor Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (SYK protein, human)
RN  - EC 2.7.10.2 (Syk Kinase)
SB  - IM
MH  - Animals
MH  - Antigens/immunology
MH  - Cell Degranulation/immunology
MH  - Humans
MH  - Hypersensitivity/immunology/metabolism
MH  - Immunoglobulin E/immunology
MH  - Intracellular Signaling Peptides and Proteins/*immunology/metabolism
MH  - Mast Cells/*immunology/metabolism/physiology
MH  - Membrane Microdomains/immunology/metabolism
MH  - Models, Immunological
MH  - Prohibitins
MH  - Protein Binding/immunology
MH  - Protein-Tyrosine Kinases/*immunology/metabolism
MH  - Receptors, IgE/*immunology/metabolism
MH  - Repressor Proteins/*immunology/metabolism
MH  - Signal Transduction/immunology
MH  - Syk Kinase
EDAT- 2013/09/12 06:00
MHDA- 2014/04/15 06:00
CRDT- 2013/09/12 06:00
PHST- 2013/09/12 06:00 [entrez]
PHST- 2013/09/12 06:00 [pubmed]
PHST- 2014/04/15 06:00 [medline]
AID - 6/292/pe29 [pii]
AID - 10.1126/scisignal.2004646 [doi]
PST - epublish
SO  - Sci Signal. 2013 Sep 10;6(292):pe29. doi: 10.1126/scisignal.2004646.