An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling

Kermit L. Carraway, Edmund A. Rossi, Masanobu Komatsu, Shari A. Price-Schiavi, Daming Huang, Pamela M. Guy, Maria E. Carvajal, Nevis Fregien, Coralie A. Carothers Carraway, Kermit L Carraway

Research output: Contribution to journalArticle

154 Citations (Scopus)

Abstract

The ErbB2 receptor tyrosine kinase plays a critical role in a variety of developmental processes, and its aberrant activation may contribute to the progression of some breast and ovarian tumors. ASGP2, a transmembrane glycoprotein found on the surface of the highly metastatic ascites 13762 rat mammary adenocarcinoma cell line, is constitutively associated with ErbB2 in these cells and in mammary tissue from pregnant rats. Expression studies indicate that ASGP2 interacts directly and specifically with ErbB2 through one of its epidermal growth factor-like domains and that the co-expression of the two proteins in the same cell dramatically facilitates their direct stable interaction. Ectopic expression of ASGP2 in human melanoma tumor cells potentiates the response of endogenous ErbB2 to the neuregulin-1 growth factor. These observations point to a novel intramembrane mechanism for the modulation of receptor tyrosine kinase activity.

Original languageEnglish (US)
Pages (from-to)5263-5266
Number of pages4
JournalJournal of Biological Chemistry
Volume274
Issue number9
DOIs
StatePublished - Feb 26 1999
Externally publishedYes

Fingerprint

Neuregulins
Receptor Protein-Tyrosine Kinases
Modulators
Rats
Tumors
Cells
Neuregulin-1
Breast
Epidermal Growth Factor
Intercellular Signaling Peptides and Proteins
Glycoproteins
Chemical activation
Modulation
Tissue
Ascites
Melanoma
Adenocarcinoma
Breast Neoplasms
Cell Line
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling. / Carraway, Kermit L.; Rossi, Edmund A.; Komatsu, Masanobu; Price-Schiavi, Shari A.; Huang, Daming; Guy, Pamela M.; Carvajal, Maria E.; Fregien, Nevis; Carothers Carraway, Coralie A.; Carraway, Kermit L.

In: Journal of Biological Chemistry, Vol. 274, No. 9, 26.02.1999, p. 5263-5266.

Research output: Contribution to journalArticle

Carraway, KL, Rossi, EA, Komatsu, M, Price-Schiavi, SA, Huang, D, Guy, PM, Carvajal, ME, Fregien, N, Carothers Carraway, CA & Carraway, KL 1999, 'An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling', Journal of Biological Chemistry, vol. 274, no. 9, pp. 5263-5266. https://doi.org/10.1074/jbc.274.9.5263
Carraway, Kermit L. ; Rossi, Edmund A. ; Komatsu, Masanobu ; Price-Schiavi, Shari A. ; Huang, Daming ; Guy, Pamela M. ; Carvajal, Maria E. ; Fregien, Nevis ; Carothers Carraway, Coralie A. ; Carraway, Kermit L. / An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 9. pp. 5263-5266.
@article{fe5bc5c9b3f441818b3c10f782a450a4,
title = "An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling",
abstract = "The ErbB2 receptor tyrosine kinase plays a critical role in a variety of developmental processes, and its aberrant activation may contribute to the progression of some breast and ovarian tumors. ASGP2, a transmembrane glycoprotein found on the surface of the highly metastatic ascites 13762 rat mammary adenocarcinoma cell line, is constitutively associated with ErbB2 in these cells and in mammary tissue from pregnant rats. Expression studies indicate that ASGP2 interacts directly and specifically with ErbB2 through one of its epidermal growth factor-like domains and that the co-expression of the two proteins in the same cell dramatically facilitates their direct stable interaction. Ectopic expression of ASGP2 in human melanoma tumor cells potentiates the response of endogenous ErbB2 to the neuregulin-1 growth factor. These observations point to a novel intramembrane mechanism for the modulation of receptor tyrosine kinase activity.",
author = "Carraway, {Kermit L.} and Rossi, {Edmund A.} and Masanobu Komatsu and Price-Schiavi, {Shari A.} and Daming Huang and Guy, {Pamela M.} and Carvajal, {Maria E.} and Nevis Fregien and {Carothers Carraway}, {Coralie A.} and Carraway, {Kermit L}",
year = "1999",
month = "2",
day = "26",
doi = "10.1074/jbc.274.9.5263",
language = "English (US)",
volume = "274",
pages = "5263--5266",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "9",

}

TY - JOUR

T1 - An intramembrane modulator of the ErbB2 receptor tyrosine kinase that potentiates neuregulin signaling

AU - Carraway, Kermit L.

AU - Rossi, Edmund A.

AU - Komatsu, Masanobu

AU - Price-Schiavi, Shari A.

AU - Huang, Daming

AU - Guy, Pamela M.

AU - Carvajal, Maria E.

AU - Fregien, Nevis

AU - Carothers Carraway, Coralie A.

AU - Carraway, Kermit L

PY - 1999/2/26

Y1 - 1999/2/26

N2 - The ErbB2 receptor tyrosine kinase plays a critical role in a variety of developmental processes, and its aberrant activation may contribute to the progression of some breast and ovarian tumors. ASGP2, a transmembrane glycoprotein found on the surface of the highly metastatic ascites 13762 rat mammary adenocarcinoma cell line, is constitutively associated with ErbB2 in these cells and in mammary tissue from pregnant rats. Expression studies indicate that ASGP2 interacts directly and specifically with ErbB2 through one of its epidermal growth factor-like domains and that the co-expression of the two proteins in the same cell dramatically facilitates their direct stable interaction. Ectopic expression of ASGP2 in human melanoma tumor cells potentiates the response of endogenous ErbB2 to the neuregulin-1 growth factor. These observations point to a novel intramembrane mechanism for the modulation of receptor tyrosine kinase activity.

AB - The ErbB2 receptor tyrosine kinase plays a critical role in a variety of developmental processes, and its aberrant activation may contribute to the progression of some breast and ovarian tumors. ASGP2, a transmembrane glycoprotein found on the surface of the highly metastatic ascites 13762 rat mammary adenocarcinoma cell line, is constitutively associated with ErbB2 in these cells and in mammary tissue from pregnant rats. Expression studies indicate that ASGP2 interacts directly and specifically with ErbB2 through one of its epidermal growth factor-like domains and that the co-expression of the two proteins in the same cell dramatically facilitates their direct stable interaction. Ectopic expression of ASGP2 in human melanoma tumor cells potentiates the response of endogenous ErbB2 to the neuregulin-1 growth factor. These observations point to a novel intramembrane mechanism for the modulation of receptor tyrosine kinase activity.

UR - http://www.scopus.com/inward/record.url?scp=0033605267&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033605267&partnerID=8YFLogxK

U2 - 10.1074/jbc.274.9.5263

DO - 10.1074/jbc.274.9.5263

M3 - Article

VL - 274

SP - 5263

EP - 5266

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 9

ER -