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Titolo:
Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration
Autore:
Bourguignon, LYW; Zhu, HB; Shao, LJ; Chen, YW;
Indirizzi:
Univ Miami, Sch Med, Dept Cell Biol & Anat, Miami, FL 33101 USA Univ Miami Miami FL USA 33101 Dept Cell Biol & Anat, Miami, FL 33101 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 1, volume: 150, anno: 2000,
pagine: 177 - 191
SICI:
0021-9525(20000710)150:1<177:AIPRSA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ERYTHROCYTE ANKYRIN; T-LYMPHOMA CELLS; GUANINE-NUCLEOTIDE EXCHANGE; INTERNAL CA2+ RELEASE; TRANSMEMBRANE GLYCOPROTEIN GP85; PLECKSTRIN HOMOLOGY DOMAIN; DBL ONCOGENE PRODUCT; ACTIN STRESS FIBERS; PLASMA-MEMBRANE; BINDING DOMAIN;
Keywords:
Tiam1; ankyrin; Rac1 signaling; invasion/migration; metastatic breast tumor cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Bourguignon, LYW Univ Miami, Sch Med, Dept Cell Biol & Anat, 1600 NW 10th Ave, Miami, FL 33101 USA Univ Miami 1600 NW 10th Ave Miami FL USA 33101 33101 USA
Citazione:
L.Y.W. Bourguignon et al., "Ankyrin-Tiam1 interaction promotes Rac1 signaling and metastatic breast tumor cell invasion and migration", J CELL BIOL, 150(1), 2000, pp. 177-191

Abstract

Tiam1 (T-lymphoma invasion and metastasis 1) is one of the known guanine nucleotide (GDP/GTP) exchange factors (GEFs) for Rho GTPases (e.g., Rad) andis expressed in breast tumor cells (e.g., SP-1 cell line). Immunoprecipitation and immunoblot analyses indicate that Tiam1 and the cytoskeletal protein, ankyrin, are physically associated as a complex in vivo. In particular,the ankyrin repeat domain (ARD) of ankyrin is responsible for Tiam1 binding. Biochemical studies and deletion mutation analyses indicate that the Il-amino acid sequence between amino acids 717 and 727 of Tiam1 ((717)GEGTDAVKRS(727)L) is the ankyrinbinding domain. Most importantly, ankyrin binding to Tiam1 activates GDP/GTP exchange on Rho GTPases (e.g., Rad). Using an Escherichia coli-derived calmodulin-binding peptide (CBP)-tagged recombinant Tiam1 (amino acids 393-728) fragment that contains the ankyrinbinding domain, we have detected a specific binding interaction between the Tiam1 (amino acids 393-738) fragment and ankyrin in vitro. This Tiam1 fragment also acts as a potent competitive inhibitor for Tiam1 binding to ankyrin. Transfection of SP-1 cell with Tiam1 cDNAs stimulates all of the following: (1) Tiam1-ankyrin association in the membrane projection; (2) Rad activation; and (3) breast tumor cell invasion and migration. Cotransfection of SP1 cells with green fluorescent protein (GFP)-tagged Tiam1 fragment cDNA and Tiam1 cDNA effectively blocks Tiam1-ankyrin colocalization in the cell membrane, and inhibits GDP/GTP exchange on Rad by ankyrin-associated Tiam1 and tumor-specific phenotypes. These findings suggest that ankyrin-Tiam1 interaction plays a pivotal role in regulating Rad signaling and cytoskeleton function required for oncogenic signaling and metastatic breast tumor cell progression.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 04:48:02