A Dual Parameter FRET Probe for Measuring PKC and PKA Activity in Living Cells
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 prot...
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| Veröffentlicht in: | Journal of the American Chemical Society 2006-01, Vol.128 (1), p.24-25 |
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| container_issue | 1 |
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| container_title | Journal of the American Chemical Society |
| container_volume | 128 |
| creator | Brumbaugh, Justin Schleifenbaum, Andreas Gasch, Alexander Sattler, Michael Schultz, Carsten |
| description | 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. |
| doi_str_mv | 10.1021/ja0562200 |
| format | Article |
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Psychology ; HeLa Cells ; Humans ; Mutagenesis, Site-Directed ; Neuroblastoma ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Phosphoproteins - chemistry ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Kinase C - metabolism ; Structure-Activity Relationship ; Transferases</subject><ispartof>Journal of the American Chemical Society, 2006-01, Vol.128 (1), p.24-25</ispartof><rights>Copyright © 2006 American Chemical Society</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a447t-cc64ff3467ca18d047881c999bb7bb3f037e9302c9c4a219f8f800da0feea4693</citedby><cites>FETCH-LOGICAL-a447t-cc64ff3467ca18d047881c999bb7bb3f037e9302c9c4a219f8f800da0feea4693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja0562200$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja0562200$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17720239$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16390103$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brumbaugh, Justin</creatorcontrib><creatorcontrib>Schleifenbaum, Andreas</creatorcontrib><creatorcontrib>Gasch, Alexander</creatorcontrib><creatorcontrib>Sattler, Michael</creatorcontrib><creatorcontrib>Schultz, Carsten</creatorcontrib><title>A Dual Parameter FRET Probe for Measuring PKC and PKA Activity in Living Cells</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>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.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Consensus Sequence</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Enzyme Activation</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fluorescence Resonance Energy Transfer - methods</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Fluorescent Dyes - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Mutagenesis, Site-Directed</subject><subject>Neuroblastoma</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinase C - metabolism</subject><subject>Structure-Activity Relationship</subject><subject>Transferases</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkEFPwkAQhTdGI4ge_ANmLx48VGd3S7c9EgQ0IhLEeNxMl11TLC3ZbY38e0sgcPH0ZvK-vJk8Qq4Z3DPg7GGJ0I04BzghbdblEHQZj05JGwB4IONItMiF98tmDXnMzkmLRSIBBqJNJj36WGNOp-hwZSrj6HA2mNOpK1NDbenoq0Ffu6z4otOXPsVi0WiP9nSV_WTVhmYFHTdTY_dNnvtLcmYx9-Zqrx3yMRzM-0_B-G303O-NAwxDWQVaR6G1IoykRhYvIJRxzHSSJGkq01RYENIkArhOdIicJTa2McACwRqDYZSIDrnb5WpXeu-MVWuXrdBtFAO17UQdOmnYmx27rtOVWRzJfQkNcLsH0GvMrcNCZ_7IScmBi-3RYMdlvjK_Bx_dt4qkkF01n76rz5GYyMkM1OyYi9qrZVm7oqnknwf_AEBxgOE</recordid><startdate>20060111</startdate><enddate>20060111</enddate><creator>Brumbaugh, Justin</creator><creator>Schleifenbaum, Andreas</creator><creator>Gasch, Alexander</creator><creator>Sattler, Michael</creator><creator>Schultz, Carsten</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20060111</creationdate><title>A Dual Parameter FRET Probe for Measuring PKC and PKA Activity in Living Cells</title><author>Brumbaugh, Justin ; Schleifenbaum, Andreas ; Gasch, Alexander ; Sattler, Michael ; Schultz, Carsten</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a447t-cc64ff3467ca18d047881c999bb7bb3f037e9302c9c4a219f8f800da0feea4693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - chemistry</topic><topic>Blood Proteins - metabolism</topic><topic>Cell Line, Tumor</topic><topic>Consensus Sequence</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>Enzyme Activation</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fluorescence Resonance Energy Transfer - methods</topic><topic>Fluorescent Dyes - chemistry</topic><topic>Fluorescent Dyes - metabolism</topic><topic>Fundamental and applied biological sciences. 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Am. Chem. Soc</addtitle><date>2006-01-11</date><risdate>2006</risdate><volume>128</volume><issue>1</issue><spage>24</spage><epage>25</epage><pages>24-25</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><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. 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| ispartof | Journal of the American Chemical Society, 2006-01, Vol.128 (1), p.24-25 |
| issn | 0002-7863 1520-5126 |
| language | eng |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Blood Proteins - chemistry Blood Proteins - metabolism Cell Line, Tumor Consensus Sequence Cyclic AMP-Dependent Protein Kinases - metabolism Enzyme Activation Enzymes and enzyme inhibitors Fluorescence Resonance Energy Transfer - methods Fluorescent Dyes - chemistry Fluorescent Dyes - metabolism Fundamental and applied biological sciences. Psychology HeLa Cells Humans Mutagenesis, Site-Directed Neuroblastoma Oligopeptides - chemistry Oligopeptides - metabolism Phosphoproteins - chemistry Phosphoproteins - metabolism Phosphorylation Protein Kinase C - metabolism Structure-Activity Relationship Transferases |
| title | A Dual Parameter FRET Probe for Measuring PKC and PKA Activity in Living Cells |
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