Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting?

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Standard

Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting? / Petrone, A; Sap, J.

In: Journal of Cell Science, Vol. 113 ( Pt 13), 2000, p. 2345-54.

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

Harvard

Petrone, A & Sap, J 2000, 'Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting?', Journal of Cell Science, vol. 113 ( Pt 13), pp. 2345-54.

APA

Petrone, A., & Sap, J. (2000). Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting? Journal of Cell Science, 113 ( Pt 13), 2345-54.

Vancouver

Petrone A, Sap J. Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting? Journal of Cell Science. 2000;113 ( Pt 13):2345-54.

Author

Petrone, A ; Sap, J. / Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting?. In: Journal of Cell Science. 2000 ; Vol. 113 ( Pt 13). pp. 2345-54.

Bibtex

@article{d319df7054a811dd8d9f000ea68e967b,
title = "Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting?",
abstract = "Transmembrane (receptor) tyrosine phosphatases are intimately involved in responses to cell-cell and cell-matrix contact. Several important issues regarding the targets and regulation of this protein family are now emerging. For example, these phosphatases exhibit complex interactions with signaling pathways involving SRC family kinases, which result from their ability to control phosphorylation of both activating and inhibitory sites in these kinases and possibly also their substrates. Similarly, integrin signaling illustrates how phosphorylation of a single protein, or the activity of a pathway, can be controlled by multiple tyrosine phosphatases, attesting to the intricate integration of these enzymes in cellular regulation. Lastly, we are starting to appreciate the roles of intracellular topology, tyrosine phosphorylation and oligomerization among the many mechanisms regulating tyrosine phosphatase activity.",
author = "A Petrone and J Sap",
note = "Keywords: Animals; Cell Communication; Humans; Protein Tyrosine Phosphatases; Receptors, Cell Surface; Signal Transduction",
year = "2000",
language = "English",
volume = "113 ( Pt 13)",
pages = "2345--54",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "The/Company of Biologists Ltd.",

}

RIS

TY - JOUR

T1 - Emerging issues in receptor protein tyrosine phosphatase function: lifting fog or simply shifting?

AU - Petrone, A

AU - Sap, J

N1 - Keywords: Animals; Cell Communication; Humans; Protein Tyrosine Phosphatases; Receptors, Cell Surface; Signal Transduction

PY - 2000

Y1 - 2000

N2 - Transmembrane (receptor) tyrosine phosphatases are intimately involved in responses to cell-cell and cell-matrix contact. Several important issues regarding the targets and regulation of this protein family are now emerging. For example, these phosphatases exhibit complex interactions with signaling pathways involving SRC family kinases, which result from their ability to control phosphorylation of both activating and inhibitory sites in these kinases and possibly also their substrates. Similarly, integrin signaling illustrates how phosphorylation of a single protein, or the activity of a pathway, can be controlled by multiple tyrosine phosphatases, attesting to the intricate integration of these enzymes in cellular regulation. Lastly, we are starting to appreciate the roles of intracellular topology, tyrosine phosphorylation and oligomerization among the many mechanisms regulating tyrosine phosphatase activity.

AB - Transmembrane (receptor) tyrosine phosphatases are intimately involved in responses to cell-cell and cell-matrix contact. Several important issues regarding the targets and regulation of this protein family are now emerging. For example, these phosphatases exhibit complex interactions with signaling pathways involving SRC family kinases, which result from their ability to control phosphorylation of both activating and inhibitory sites in these kinases and possibly also their substrates. Similarly, integrin signaling illustrates how phosphorylation of a single protein, or the activity of a pathway, can be controlled by multiple tyrosine phosphatases, attesting to the intricate integration of these enzymes in cellular regulation. Lastly, we are starting to appreciate the roles of intracellular topology, tyrosine phosphorylation and oligomerization among the many mechanisms regulating tyrosine phosphatase activity.

M3 - Journal article

C2 - 10852814

VL - 113 ( Pt 13)

SP - 2345

EP - 2354

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

ER -

ID: 5069688