Research ExplorerPublicationsHigh-throughput phosphotyrosine profiling using SH2 domains.

High-throughput phosphotyrosine profiling using SH2 domains.

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High-throughput phosphotyrosine profiling using SH2 domains. / Machida, Kazuya; Thompson, Christopher M; Dierck, Kevin; Jablonowski, Karl; Kärkkäinen, Satu; Liu, Bernard; Zhang, Haimin; Nash, Piers D; Newman, Debra K; Nollau, Peter; Pawson, Tony; Renkema, G Herma; Saksela, Kalle; Schiller, Martin R; Shin, Dong-Guk; Mayer, Bruce J.

In: MOL CELL, Vol. 26, No. 6, 6, 2007, p. 899-915.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Machida, K, Thompson, CM, Dierck, K, Jablonowski, K, Kärkkäinen, S, Liu, B, Zhang, H, Nash, PD, Newman, DK, Nollau, P, Pawson, T, Renkema, GH, Saksela, K, Schiller, MR, Shin, D-G & Mayer, BJ 2007, 'High-throughput phosphotyrosine profiling using SH2 domains.', MOL CELL, vol. 26, no. 6, 6, pp. 899-915. <http://www.ncbi.nlm.nih.gov/pubmed/17588523?dopt=Citation>

APA

Machida, K., Thompson, C. M., Dierck, K., Jablonowski, K., Kärkkäinen, S., Liu, B., Zhang, H., Nash, P. D., Newman, D. K., Nollau, P., Pawson, T., Renkema, G. H., Saksela, K., Schiller, M. R., Shin, D-G., & Mayer, B. J. (2007). High-throughput phosphotyrosine profiling using SH2 domains. MOL CELL, 26(6), 899-915. [6]. http://www.ncbi.nlm.nih.gov/pubmed/17588523?dopt=Citation

Vancouver

Machida K, Thompson CM, Dierck K, Jablonowski K, Kärkkäinen S, Liu B et al. High-throughput phosphotyrosine profiling using SH2 domains. MOL CELL. 2007;26(6):899-915. 6.

Bibtex

@article{311d4ef7f17e434881e422af30936ad6,
title = "High-throughput phosphotyrosine profiling using SH2 domains.",
abstract = "Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major consequences of tyrosine phosphorylation is the creation of binding sites for proteins containing Src homology 2 (SH2) domains. To profile the global tyrosine phosphorylation state of the cell, we have developed proteomic binding assays encompassing nearly the full complement of human SH2 domains. Here we provide a global view of SH2 domain binding to cellular proteins based on large-scale far-western analyses. We also use reverse-phase protein arrays to generate comprehensive, quantitative SH2 binding profiles for phosphopeptides, recombinant proteins, and entire proteomes. As an example, we profiled the adhesion-dependent SH2 binding interactions in fibroblasts and identified specific focal adhesion complex proteins whose tyrosine phosphorylation and binding to SH2 domains are modulated by adhesion. These results demonstrate that high-throughput comprehensive SH2 profiling provides valuable mechanistic insights into tyrosine kinase signaling pathways.",
author = "Kazuya Machida and Thompson, {Christopher M} and Kevin Dierck and Karl Jablonowski and Satu K{\"a}rkk{\"a}inen and Bernard Liu and Haimin Zhang and Nash, {Piers D} and Newman, {Debra K} and Peter Nollau and Tony Pawson and Renkema, {G Herma} and Kalle Saksela and Schiller, {Martin R} and Dong-Guk Shin and Mayer, {Bruce J}",
year = "2007",
language = "Deutsch",
volume = "26",
pages = "899--915",
journal = "MOL CELL",
issn = "1097-2765",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - High-throughput phosphotyrosine profiling using SH2 domains.

AU - Machida, Kazuya

AU - Thompson, Christopher M

AU - Dierck, Kevin

AU - Jablonowski, Karl

AU - Kärkkäinen, Satu

AU - Liu, Bernard

AU - Zhang, Haimin

AU - Nash, Piers D

AU - Newman, Debra K

AU - Nollau, Peter

AU - Pawson, Tony

AU - Renkema, G Herma

AU - Saksela, Kalle

AU - Schiller, Martin R

AU - Shin, Dong-Guk

AU - Mayer, Bruce J

PY - 2007

Y1 - 2007

N2 - Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major consequences of tyrosine phosphorylation is the creation of binding sites for proteins containing Src homology 2 (SH2) domains. To profile the global tyrosine phosphorylation state of the cell, we have developed proteomic binding assays encompassing nearly the full complement of human SH2 domains. Here we provide a global view of SH2 domain binding to cellular proteins based on large-scale far-western analyses. We also use reverse-phase protein arrays to generate comprehensive, quantitative SH2 binding profiles for phosphopeptides, recombinant proteins, and entire proteomes. As an example, we profiled the adhesion-dependent SH2 binding interactions in fibroblasts and identified specific focal adhesion complex proteins whose tyrosine phosphorylation and binding to SH2 domains are modulated by adhesion. These results demonstrate that high-throughput comprehensive SH2 profiling provides valuable mechanistic insights into tyrosine kinase signaling pathways.

AB - Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major consequences of tyrosine phosphorylation is the creation of binding sites for proteins containing Src homology 2 (SH2) domains. To profile the global tyrosine phosphorylation state of the cell, we have developed proteomic binding assays encompassing nearly the full complement of human SH2 domains. Here we provide a global view of SH2 domain binding to cellular proteins based on large-scale far-western analyses. We also use reverse-phase protein arrays to generate comprehensive, quantitative SH2 binding profiles for phosphopeptides, recombinant proteins, and entire proteomes. As an example, we profiled the adhesion-dependent SH2 binding interactions in fibroblasts and identified specific focal adhesion complex proteins whose tyrosine phosphorylation and binding to SH2 domains are modulated by adhesion. These results demonstrate that high-throughput comprehensive SH2 profiling provides valuable mechanistic insights into tyrosine kinase signaling pathways.

M3 - SCORING: Zeitschriftenaufsatz

VL - 26

SP - 899

EP - 915

JO - MOL CELL

JF - MOL CELL

SN - 1097-2765

IS - 6

M1 - 6

ER -