Direct binding of the EGF-like domain of neuregulin-1 to integrins (αvβ3 and α6β4) is involved in neuregulin-1/ErbB signaling

Journal of Biological Chemistry

Volumn 285, Issue 41, 2010, Pages 31388-31398

  Ieguchi, Katsuaki ^a   Fujita, Masaaki ^a   Ma, Zi ^a   Davari, Parastoo ^a   Taniguchi, Yukimasa ^b   Sekiguchi, Kiyotoshi ^b   Wang, Bobby ^a   Takada, Yoko K ^a   Takada, Yoshikazu ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CROSSTALK; GLYCOPROTEINS; PEPTIDES; PHOSPHORYLATION;

CANCER CELLS; CURRENT MODELS; DOCKING SIMULATIONS; EXTRACELLULAR MATRICES; GROWTH FACTOR; HUMAN BREAST CANCER CELLS; INTEGRIN BINDING; INTEGRINS; MULTI DOMAINS; NEUREGULIN; TERNARY COMPLEX;

SIGNALING;

ALPHA6BETA4 INTEGRIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 3; GLUTAMIC ACID; LYSINE; MITOGEN ACTIVATED PROTEIN KINASE 1; NEU DIFFERENTIATION FACTOR; PROTEIN KINASE B; VITRONECTIN RECEPTOR; MAPK1 PROTEIN, HUMAN; MITOGEN ACTIVATED PROTEIN KINASE 3; NRG1 PROTEIN, HUMAN; PROTEIN BINDING;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING SITE; CANCER CELL; CELL STIMULATION; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVATION; FEMALE; HUMAN; HUMAN CELL; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; AMINO ACID SUBSTITUTION; ANIMAL; CHO CELL LINE; CRICETULUS; GENETICS; HAMSTER; K562 CELL LINE; METABOLISM; MISSENSE MUTATION; PHOSPHORYLATION; PROTEIN QUATERNARY STRUCTURE;

AMINO ACID SUBSTITUTION; ANIMALS; CHO CELLS; CRICETINAE; CRICETULUS; HUMANS; INTEGRIN ALPHAVBETA3; K562 CELLS; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; MUTATION, MISSENSE; NEUREGULIN-1; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTO-ONCOGENE PROTEINS C-AKT; RECEPTOR, ERBB-3; SIGNAL TRANSDUCTION;

EID: 77957765881     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.113878     Document Type: Article

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