PMID- 10473551
OWN - NLM
STAT- MEDLINE
DCOM- 19991007
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 37
DP  - 1999 Sep 10
TI  - Cdc42 and Rac1 regulate the interaction of IQGAP1 with beta-catenin.
PG  - 26044-50
AB  - IQGAP1, a target of Cdc42 and Rac1 small GTPases, directly interacts with
      beta-catenin and negatively regulates E-cadherin-mediated cell-cell adhesion by
      dissociating alpha-catenin from the cadherin-catenin complex in vivo (Kuroda, S.,
      Fukata, M., Nakagawa, M., Fujii, K., Nakamura, T., Ookubo, T., Izawa, I., Nagase,
      T., Nomura, N., Tani, H., Shoji, I., Matsuura, Y., Yonehara, S., and Kaibuchi, K.
      (1998) Science 281, 832-835). Here we investigated how Cdc42 and Rac1 regulate
      the IQGAP1 function. IQGAP1 interacted with the amino-terminal region (amino
      acids 1-183) of beta-catenin, which contains the alpha-catenin-binding domain.
      IQGAP1 dissociated alpha-catenin from the beta-catenin-alpha-catenin complex in a
      dose-dependent manner in vitro. Guanosine 5'-(3-O-thio)triphosphate
      (GTPgammaS).glutathione S-transferase (GST)-Cdc42 and GTPgammaS. GST-Rac1
      inhibited the binding of IQGAP1 to beta-catenin in a dose-dependent manner in
      vitro, whereas neither GDP.GST-Cdc42, GDP. GST-Rac1, nor GTPgammaS.GST-RhoA did. 
      The coexpression of dominant active Cdc42 with IQGAP1 suppressed the dissociation
      of alpha-catenin from the cadherin-catenin complex induced by the overexpression 
      of IQGAP1 in L cells expressing E-cadherin (EL cells). Consistent with this, the 
      overexpression of either dominant negative Cdc42 or Rac1 resulted in the
      reduction of E-cadherin-mediated cell adhesive activity in EL cells. These
      results indicate that Cdc42 and Rac1 negatively regulate the IQGAP1 function by
      inhibiting the interaction of IQGAP1 with beta-catenin, leading to stabilization 
      of the cadherin-catenin complex.
FAU - Fukata, M
AU  - Fukata M
AD  - Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 
      630-0101, Japan.
FAU - Kuroda, S
AU  - Kuroda S
FAU - Nakagawa, M
AU  - Nakagawa M
FAU - Kawajiri, A
AU  - Kawajiri A
FAU - Itoh, N
AU  - Itoh N
FAU - Shoji, I
AU  - Shoji I
FAU - Matsuura, Y
AU  - Matsuura Y
FAU - Yonehara, S
AU  - Yonehara S
FAU - Fujisawa, H
AU  - Fujisawa H
FAU - Kikuchi, A
AU  - Kikuchi A
FAU - Kaibuchi, K
AU  - Kaibuchi K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (IQ motif containing GTPase activating protein 1)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (beta Catenin)
RN  - 0 (ras GTPase-Activating Proteins)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (rac GTP-Binding Proteins)
SB  - IM
MH  - Carrier Proteins/*metabolism
MH  - Cell Cycle Proteins/*metabolism
MH  - Cytoskeletal Proteins/*metabolism
MH  - GTP-Binding Proteins/*metabolism
MH  - Protein Binding
MH  - Recombinant Proteins/metabolism
MH  - *Trans-Activators
MH  - beta Catenin
MH  - rac GTP-Binding Proteins
MH  - *ras GTPase-Activating Proteins
EDAT- 1999/09/03 00:00
MHDA- 1999/09/03 00:01
CRDT- 1999/09/03 00:00
PHST- 1999/09/03 00:00 [pubmed]
PHST- 1999/09/03 00:01 [medline]
PHST- 1999/09/03 00:00 [entrez]
AID - 10.1074/jbc.274.37.26044 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Sep 10;274(37):26044-50. doi: 10.1074/jbc.274.37.26044.