A dual parameter FRET probe for measuring PKC and PKA activity in living cells

Justin Brumbaugh; Andreas Schleifenbaum; Alexander Gasch; Michael Sattler; Carsten Schultz

doi:10.1021/ja0562200

A dual parameter FRET probe for measuring PKC and PKA activity in living cells

Justin Brumbaugh, Andreas Schleifenbaum, Alexander Gasch, Michael Sattler, Carsten Schultz

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

19 Scopus citations

Abstract

Cell function is regulated by complex and often interdependent networks of signaling molecules. To accurately describe these networks, it is important to monitor multiple signals in parallel. To this end, we have developed a genetically encoded, FRET-based probe that independently monitors both protein kinase A (PKA) and protein kinase C (PKC) activity in vivo. Artificial as well as physiological stimulants produced a negative or positive change in FRET efficiency following PKA or PKC activation, respectively. Mutations of the phosphate-accepting amino acids of the PKC substrate yielded a probe that was sensitive to PKA activation alone.

Original language	English (US)
Pages (from-to)	24-25
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	128
Issue number	1
DOIs	https://doi.org/10.1021/ja0562200
State	Published - Jan 11 2006
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja0562200

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AU - Schleifenbaum, Andreas

AU - Gasch, Alexander

AU - Sattler, Michael

AU - Schultz, Carsten

PY - 2006/1/11

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AB - Cell function is regulated by complex and often interdependent networks of signaling molecules. To accurately describe these networks, it is important to monitor multiple signals in parallel. To this end, we have developed a genetically encoded, FRET-based probe that independently monitors both protein kinase A (PKA) and protein kinase C (PKC) activity in vivo. Artificial as well as physiological stimulants produced a negative or positive change in FRET efficiency following PKA or PKC activation, respectively. Mutations of the phosphate-accepting amino acids of the PKC substrate yielded a probe that was sensitive to PKA activation alone.

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A dual parameter FRET probe for measuring PKC and PKA activity in living cells

Abstract

ASJC Scopus subject areas

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