PMID- 10092676
OWN - NLM
STAT- MEDLINE
DCOM- 19990427
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 14
DP  - 1999 Apr 2
TI  - Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST
      (PTP-PEST) through its LIM 3 domain.
PG  - 9847-53
AB  - The Hic-5 protein is encoded by a transforming growth factor-beta1- and hydrogen 
      peroxide-inducible gene, hic-5, and has striking similarity to paxillin,
      especially in their C-terminal LIM domains. Like paxillin, Hic-5 is localized in 
      focal adhesion plaques in association with focal adhesion kinase in cultured
      fibroblasts. We carried out yeast two-hybrid screening to identify cellular
      factors that form a complex with Hic-5 using its LIM domains as a bait, and we
      identified a cytoplasmic tyrosine phosphatase (PTP-PEST) as one of the partners
      of Hic-5. These two proteins are associated in mammalian cells. From in vitro
      binding experiments using deletion and point mutations, it was demonstrated that 
      the essential domain in Hic-5 for the binding was LIM 3. As for PTP-PEST, one of 
      the five proline-rich sequences found on PTP-PEST, Pro-2, was identified as the
      binding site for Hic-5 in in vitro binding assays. Paxillin also binds to the
      Pro-2 domain of PTP-PEST. In conclusion, Hic-5 may participate in the regulation 
      of signaling cascade through its interaction with distinct tyrosine kinases and
      phosphatases.
FAU - Nishiya, N
AU  - Nishiya N
AD  - Department of Microbiology, Showa University School of Pharmaceutical Sciences,
      Hatanodai 1-5-8, Shinagawa-ku, Tokyo, Japan.
FAU - Iwabuchi, Y
AU  - Iwabuchi Y
FAU - Shibanuma, M
AU  - Shibanuma M
FAU - Cote, J F
AU  - Cote JF
FAU - Tremblay, M L
AU  - Tremblay ML
FAU - Nose, K
AU  - Nose 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 (Cytoskeletal Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Homeodomain Proteins)
RN  - 0 (LIM Domain Proteins)
RN  - 0 (LIM-Homeodomain Proteins)
RN  - 0 (Lhx3 protein)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Tgfb1i1 protein, mouse)
RN  - 0 (Transcription Factors)
RN  - 0 (Transforming Growth Factor beta)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 12)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Ptpn12 protein, mouse)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - Cells, Cultured
MH  - Cytoskeletal Proteins/genetics/*metabolism
MH  - DNA, Complementary/chemistry/isolation & purification
MH  - DNA-Binding Proteins/genetics/*metabolism
MH  - Homeodomain Proteins/*metabolism
MH  - LIM Domain Proteins
MH  - LIM-Homeodomain Proteins
MH  - Mice
MH  - Muscles/metabolism
MH  - Nerve Tissue Proteins/*metabolism
MH  - Protein Binding
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 12
MH  - Protein Tyrosine Phosphatases/genetics/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Structure-Activity Relationship
MH  - Transcription Factors
MH  - Transforming Growth Factor beta/*metabolism
MH  - *Zinc Fingers
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
AID - 10.1074/jbc.274.14.9847 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 2;274(14):9847-53. doi: 10.1074/jbc.274.14.9847.