Mechanism of persistent protein kinase D1 translocation and activation
The specificity of many signal transduction pathways relies on the spatiotemporal features of each signaling step. G protein-coupled receptor-mediated activation of protein kinases leads to diverse cellular effects. Upon receptor activation, PKD1 and several C-type protein kinases (PKCs), translocate to the plasma membrane and become catalytically active. Here we show that, unlike PKCs, PKD1 remains active at the membrane for hours. The two DAG binding C1 domains of PKD1 have distinct functional roles in targeting and maintaining PKD1 at the plasma membrane. C1A achieves fast, maximal, and reversible translocation, while C1B translocates partially, but persistently, to the plasma membrane. The persistent localization requires the C1B domain of PKD1, which binds Galphaq. We incorporate the kinetics of PKD1 translocation into a three-state model that suggests how PKD1 binding to DAG and Galphaq uniquely encodes frequency-dependent PKD1 signaling.
| Medienart: |
Artikel |
|---|
| Erscheinungsjahr: |
2003 |
|---|---|
| Erschienen: |
2003 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:4 |
|---|---|
| Enthalten in: |
Developmental cell - 4(2003), 4 vom: 05. Apr., Seite 561-74 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Oancea, Elena [VerfasserIn] |
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| Anmerkungen: |
Date Completed 16.06.2003 Date Revised 07.11.2019 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM124612679 |
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| 245 | 1 | 0 | |a Mechanism of persistent protein kinase D1 translocation and activation |
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| 500 | |a Date Completed 16.06.2003 | ||
| 500 | |a Date Revised 07.11.2019 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a The specificity of many signal transduction pathways relies on the spatiotemporal features of each signaling step. G protein-coupled receptor-mediated activation of protein kinases leads to diverse cellular effects. Upon receptor activation, PKD1 and several C-type protein kinases (PKCs), translocate to the plasma membrane and become catalytically active. Here we show that, unlike PKCs, PKD1 remains active at the membrane for hours. The two DAG binding C1 domains of PKD1 have distinct functional roles in targeting and maintaining PKD1 at the plasma membrane. C1A achieves fast, maximal, and reversible translocation, while C1B translocates partially, but persistently, to the plasma membrane. The persistent localization requires the C1B domain of PKD1, which binds Galphaq. We incorporate the kinetics of PKD1 translocation into a three-state model that suggests how PKD1 binding to DAG and Galphaq uniquely encodes frequency-dependent PKD1 signaling | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Research Support, U.S. Gov't, P.H.S. | |
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| 650 | 7 | |a Recombinant Fusion Proteins |2 NLM | |
| 650 | 7 | |a protein kinase D |2 NLM | |
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| 700 | 1 | |a Bezzerides, Vassilios J |e verfasserin |4 aut | |
| 700 | 1 | |a Greka, Anna |e verfasserin |4 aut | |
| 700 | 1 | |a Clapham, David E |e verfasserin |4 aut | |
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