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Titolo:
Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF
Autore:
Taya, S; Inagaki, N; Sengiku, H; Makino, H; Iwamatsu, A; Urakawa, I; Nagao, K; Kataoka, S; Kaibuchi, K;
Indirizzi:
Nagoya Univ, Grad Sch Med, Dept Cell Pharmacol, Showa Ku, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 a Ku, Nagoya, Aichi 4668550, Japan Nara Inst Sci & Technol, Div Signal Transduct, Ikoma 6300101, Japan Nara Inst Sci & Technol Ikoma Japan 6300101 nsduct, Ikoma 6300101, Japan JST, PREST, Recognit & Format, Kumamoto 8600012, Japan JST Kumamoto Japan 8600012 T, Recognit & Format, Kumamoto 8600012, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan Kirin Brewery Co Ltd, Pharmaceut Res Lab, Takasaki, Gumma 3701295, Japan Kirin Brewery Co Ltd Takasaki Gumma Japan 3701295 i, Gumma 3701295, Japan
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 5, volume: 155, anno: 2001,
pagine: 809 - 819
SICI:
0021-9525(20011126)155:5<809:DIOIGF>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOTIDE EXCHANGE FACTOR; BINDING PROTEIN-RHO; HETEROTRIMERIC G-PROTEINS; SERINE THREONINE KINASE; SMOOTH-MUSCLE; SIGNAL-TRANSDUCTION; CELL-ADHESION; ONCOGENIC RAS; P115 RHOGEF; KB-CELLS;
Keywords:
IGF-1; Rho; LARG; PDZ domain; GEF;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Kaibuchi, K Nagoya Univ, Grad Sch Med, Dept Cell Pharmacol, Showa Ku, 65 Tsurumai, Nagoya, Aichi 4668550, Japan Nagoya Univ 65 Tsurumai Nagoya Aichi Japan 4668550 8550, Japan
Citazione:
S. Taya et al., "Direct interaction of insulin-like growth factor-1 receptor with leukemia-associated RhoGEF", J CELL BIOL, 155(5), 2001, pp. 809-819

Abstract

Insulin-like growth factor (IGF)-1 plays crucial roles in growth control and rearrangements of the cytoskeleton. IGF-1 binds to the IGF-1 receptor and thereby induces the autophosphorylation of this receptor at its tyrosine residues, The phosphorylation of the IGF-1 receptor is thought to initiate a cascade of events. Although various signaling molecules have been identified, they appear to interact with the tyrosine-phosphorylated IGF-1 receptor. Here, we identified leukemia-associated Rho guanine nucleotide exchange factor (GEF) (LARG), which contains the PSD-95/Dlg/ZO-1 (PDZ), regulator ofG protein signaling (RGS), Dbl homology, and pleckstrin homology domains, as a nonphosphorylated IGF-1 receptor-interacting molecule. LARG formed a complex with the IGF-1 receptor in vivo, and the PDZ domain of LARG interacted directly with the COOH-terminal domain of IGF-1 receptor in vitro. LARG had an exchange activity for Rho in vitro and induced the formation of stress fibers in NIH 3T3 fibroblasts. When MDCKII epithelial cells were treatedwith IGF-1, Rho and its effector Rho-associated kinase (Rho-kinase) were activated and actin stress fibers were enhanced. Furthermore, the IGF-1-induced Rho-kinase activation and the enhancement of stress fibers were inhibited by ectopic expression of the PDZ and RGS domains of LARG. Taken together, these results indicate that IGF-1 activates the Rho/Rho-kinase pathway via a LARG/IGF-1 receptor complex and thereby regulates cytoskeletal rearrangements.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 11:00:39