Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL

Ravi Salgia, Beatrice Brunkhorst, Evan Pisick, Jian Liang Li, Su Hao Lo, Lan Bo Chen, James D. Griffin

Research output: Contribution to journalArticle

148 Citations (Scopus)

Abstract

The BCR/ABL oncogene causes chronic myelogenous leukemia (CML) in humans and induces growth factor independence of hematopoietic cell lines in tissue culture. p210BCR/ABL is localized at least in part to the cytoskeleton, and has been shown to interact directly with actin filaments through an actin binding domain located in the C-terminus of ABL. CML cells have reduced adhesion to some extracellular matrix components but the mechanism of this phenomenon is unknown. In this study we examined tyrosine phosphorylation of focal adhesion proteins in cells expressing p210BCR/ABL. An interleukin-3 (IL-3)-dependent cell line, 32Dc13, was transformed with a BCR/ABL cDNA, and the patterns of localization, expression, and tyrosine phosphorylation of focal adhesion proteins were compared among untransformed 32Dc13 cells with and without IL-3 stimulation and BCR/ABL-transformed 32Dc13 cells. Of the focal adhesion proteins examined, only paxillin exhibited tyrosine phosphorylation in response to IL-3; while in cells transformed by p210BCR/ABL, paxillin, vinculin, p125FAK, talin and tensin were constitutively tyrosine phosphorylated. IL-3 induced a transient association between paxillin and vinculin, while in BCR/ABL-transformed cells, several proteins coimmunoprecipitated with paxillin, including vinculin, p125FAK, talin and tensin. Pseudopodia enriched in focal adhesion proteins were transiently detected in 32Dc13 cells in response to IL-3, but constitutively detected in cells expressing p210BCR/ABL. p210BCR/ABL protein was also found concentrated in punctate structures adjacent to the cell membrane in myeloid cell lines, which often contained vinculin and paxillin. Since the focal adhesion is where the interaction between integrins and actin filaments is believed to occur, the observed effect of p210BCR/ABL on food adhesion protein interactions in myeloid cell lines could contribute to the adhesion defects in CML cells.

Original languageEnglish (US)
Pages (from-to)1149-1155
Number of pages7
JournalOncogene
Volume11
Issue number6
StatePublished - Sep 21 1995
Externally publishedYes

Fingerprint

Focal Adhesions
Myeloid Cells
Tyrosine
Paxillin
Phosphorylation
Cell Line
Interleukin-3
Vinculin
Proteins
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Talin
Actin Cytoskeleton
Pseudopodia
Cytoskeleton
Oncogenes
Integrins
Extracellular Matrix
Actins
Intercellular Signaling Peptides and Proteins
Complementary DNA

Keywords

  • Actin
  • Cytoskeletal proteins
  • p210
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

Cite this

Salgia, R., Brunkhorst, B., Pisick, E., Li, J. L., Lo, S. H., Chen, L. B., & Griffin, J. D. (1995). Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL Oncogene, 11(6), 1149-1155.

Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL . / Salgia, Ravi; Brunkhorst, Beatrice; Pisick, Evan; Li, Jian Liang; Lo, Su Hao; Chen, Lan Bo; Griffin, James D.

In: Oncogene, Vol. 11, No. 6, 21.09.1995, p. 1149-1155.

Research output: Contribution to journalArticle

Salgia, R, Brunkhorst, B, Pisick, E, Li, JL, Lo, SH, Chen, LB & Griffin, JD 1995, 'Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL ', Oncogene, vol. 11, no. 6, pp. 1149-1155.
Salgia R, Brunkhorst B, Pisick E, Li JL, Lo SH, Chen LB et al. Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL Oncogene. 1995 Sep 21;11(6):1149-1155.
Salgia, Ravi ; Brunkhorst, Beatrice ; Pisick, Evan ; Li, Jian Liang ; Lo, Su Hao ; Chen, Lan Bo ; Griffin, James D. / Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL In: Oncogene. 1995 ; Vol. 11, No. 6. pp. 1149-1155.
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AB - The BCR/ABL oncogene causes chronic myelogenous leukemia (CML) in humans and induces growth factor independence of hematopoietic cell lines in tissue culture. p210BCR/ABL is localized at least in part to the cytoskeleton, and has been shown to interact directly with actin filaments through an actin binding domain located in the C-terminus of ABL. CML cells have reduced adhesion to some extracellular matrix components but the mechanism of this phenomenon is unknown. In this study we examined tyrosine phosphorylation of focal adhesion proteins in cells expressing p210BCR/ABL. An interleukin-3 (IL-3)-dependent cell line, 32Dc13, was transformed with a BCR/ABL cDNA, and the patterns of localization, expression, and tyrosine phosphorylation of focal adhesion proteins were compared among untransformed 32Dc13 cells with and without IL-3 stimulation and BCR/ABL-transformed 32Dc13 cells. Of the focal adhesion proteins examined, only paxillin exhibited tyrosine phosphorylation in response to IL-3; while in cells transformed by p210BCR/ABL, paxillin, vinculin, p125FAK, talin and tensin were constitutively tyrosine phosphorylated. IL-3 induced a transient association between paxillin and vinculin, while in BCR/ABL-transformed cells, several proteins coimmunoprecipitated with paxillin, including vinculin, p125FAK, talin and tensin. Pseudopodia enriched in focal adhesion proteins were transiently detected in 32Dc13 cells in response to IL-3, but constitutively detected in cells expressing p210BCR/ABL. p210BCR/ABL protein was also found concentrated in punctate structures adjacent to the cell membrane in myeloid cell lines, which often contained vinculin and paxillin. Since the focal adhesion is where the interaction between integrins and actin filaments is believed to occur, the observed effect of p210BCR/ABL on food adhesion protein interactions in myeloid cell lines could contribute to the adhesion defects in CML cells.

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