A rapid method for determining protein kinase phosphorylation specificity

Jessica E. Hutti; Emily T. Jarrell; James D. Chang; Derek W. Abbott; Peter Storz; Alex Toker; Lewis C. Cantley; Benjamin E. Turk

doi:10.1038/nmeth708

A rapid method for determining protein kinase phosphorylation specificity

Jessica E. Hutti, Emily T. Jarrell, James D. Chang, Derek W. Abbott, Peter Storz, Alex Toker, Lewis C. Cantley, Benjamin E. Turk

Cancer Biology

Research output: Contribution to journal › Article › peer-review

266 Scopus citations

Abstract

Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

Original language	English (US)
Pages (from-to)	27-29
Number of pages	3
Journal	Nature Methods
Volume	1
Issue number	1
DOIs	https://doi.org/10.1038/nmeth708
State	Published - Oct 2004

ASJC Scopus subject areas

Biotechnology
Biochemistry
Molecular Biology
Cell Biology

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10.1038/nmeth708

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abstract = "Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.",

author = "Hutti, {Jessica E.} and Jarrell, {Emily T.} and Chang, {James D.} and Abbott, {Derek W.} and Peter Storz and Alex Toker and Cantley, {Lewis C.} and Turk, {Benjamin E.}",

note = "Funding Information: We thank N. Ahn for providing the active MKK1 clone and T. Obata for preparation of recombinant Akt used in pilot studies. This work was supported by US National Institutes Health grants GM56203 to L.C.C. and CA75134 to A.T. B.E.T. is a Leukemia and Lymphoma Society Special Fellow.",

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AU - Hutti, Jessica E.

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AU - Chang, James D.

AU - Abbott, Derek W.

AU - Storz, Peter

AU - Toker, Alex

AU - Cantley, Lewis C.

AU - Turk, Benjamin E.

N1 - Funding Information: We thank N. Ahn for providing the active MKK1 clone and T. Obata for preparation of recombinant Akt used in pilot studies. This work was supported by US National Institutes Health grants GM56203 to L.C.C. and CA75134 to A.T. B.E.T. is a Leukemia and Lymphoma Society Special Fellow.

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AB - Selection of target substrates by protein kinases is strongly influenced by the amino acid sequence surrounding the phosphoacceptor site. Identification of the preferred peptide phosphorylation motif for a given kinase permits the production of efficient peptide substrates and greatly simplifies the mapping of phosphorylation sites in protein substrates. Here we describe a combinatorial peptide library method that allows rapid generation of phosphorylation motifs for serine/threonine kinases.

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A rapid method for determining protein kinase phosphorylation specificity

Abstract

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