PMID- 21168390
OWN - NLM
STAT- MEDLINE
DCOM- 20110311
LR  - 20131121
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Linking)
VI  - 404
IP  - 3
DP  - 2011 Jan 21
TI  - Insulin receptor substrates form high-molecular-mass complexes that modulate 
      their availability to insulin/insulin-like growth factor-I receptor tyrosine 
      kinases.
PG  - 767-73
LID - 10.1016/j.bbrc.2010.12.045 [doi]
AB  - Insulin receptor substrates (IRSs) are phosphorylated by activated 
      insulin/insulin-like growth factor (IGF)-I receptor tyrosine kinases. 
      Phosphotyrosyl IRSs are recognized by signaling molecules possessing src homology 
      region 2 (SH2) domains, which mediate various insulin/IGF bioactivities. However, 
      we have shown that IRSs are also associated with other proteins by a 
      phosphotyrosine-independent mechanism. Here, we demonstrated that IRSs form 
      high-molecular-mass complexes (we named these complexes IRSomes) with various 
      proteins and we elucidated their possible roles. Blue native-polyacrylamide gel 
      electrophoresis of cell lysates revealed IRSome formation. Some proteins 
      associated with IRSs in IRS-isoform-, cell-type-, or stimulus-specific manners. 
      Results of the in vitro tyrosine phosphorylation assay indicated that tyrosine 
      phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was 
      contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-alpha. Also, 
      tyrosine phosphorylation of IRS-2 by IGF-I receptor was increased when IRS-2 was 
      contained in IRSomes prepared from FRTL-5 thyrocytes treated with dibutyryl cAMP. 
      These results demonstrated that cytokine/hormone-induced formation of IRSomes 
      modulates availability of IRSs to receptor tyrosine kinases.
CI  - Copyright (c) 2010 Elsevier Inc. All rights reserved.
FAU - Fukushima, Toshiaki
AU  - Fukushima T
AD  - Department of Animal Sciences, Graduate School of Agriculture and Life Sciences, 
      The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
FAU - Arai, Toshiya
AU  - Arai T
FAU - Ariga-Nedachi, Miyako
AU  - Ariga-Nedachi M
FAU - Okajima, Hiroshi
AU  - Okajima H
FAU - Ooi, Yuko
AU  - Ooi Y
FAU - Iijima, Yumi
AU  - Iijima Y
FAU - Sone, Meri
AU  - Sone M
FAU - Cho, Yoshitake
AU  - Cho Y
FAU - Ando, Yasutoshi
AU  - Ando Y
FAU - Kasahara, Kohei
AU  - Kasahara K
FAU - Ozoe, Atsufumi
AU  - Ozoe A
FAU - Yoshihara, Hidehito
AU  - Yoshihara H
FAU - Chida, Kazuhiro
AU  - Chida K
FAU - Okada, Shigeru
AU  - Okada S
FAU - Kopchick, John J
AU  - Kopchick JJ
FAU - Asano, Tomoichiro
AU  - Asano T
FAU - Hakuno, Fumihiko
AU  - Hakuno F
FAU - Takahashi, Shin-Ichiro
AU  - Takahashi S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20101217
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Insulin)
RN  - 0 (Insulin Receptor Substrate Proteins)
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 42HK56048U (Tyrosine)
RN  - 63X7MBT2LQ (Bucladesine)
RN  - EC 2.7.10.1 (Receptor, IGF Type 1)
SB  - IM
MH  - 3T3-L1 Cells
MH  - Adipocytes/*metabolism
MH  - Animals
MH  - Bucladesine/metabolism
MH  - HEK293 Cells
MH  - Humans
MH  - Insulin/*metabolism
MH  - Insulin Receptor Substrate Proteins/*metabolism
MH  - Mice
MH  - Multiprotein Complexes/*metabolism
MH  - Phosphorylation
MH  - Receptor, IGF Type 1/*metabolism
MH  - Thyroid Gland/cytology/metabolism
MH  - Tumor Necrosis Factor-alpha/pharmacology
MH  - Tyrosine/metabolism
EDAT- 2010/12/21 06:00
MHDA- 2011/03/12 06:00
CRDT- 2010/12/21 06:00
PHST- 2010/12/07 00:00 [received]
PHST- 2010/12/08 00:00 [accepted]
PHST- 2010/12/21 06:00 [entrez]
PHST- 2010/12/21 06:00 [pubmed]
PHST- 2011/03/12 06:00 [medline]
AID - S0006-291X(10)02283-7 [pii]
AID - 10.1016/j.bbrc.2010.12.045 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2011 Jan 21;404(3):767-73. doi: 
      10.1016/j.bbrc.2010.12.045. Epub 2010 Dec 17.