Neutrophils play a key role in host-defence mechanisms against invading pathogens, using their capacity to migrate, engulf micro-organisms and produce toxic radicals. Protein kinase C (PKC) isotypes are important intracellular regulators of these processes in neutrophils. PKC isotypes themselves are controlled by interactions with lipids, Ca2+ and proteins. The C2-like domain of PKC-δ (δC2) has been identified as a protein-interaction domain in this PKC isotype. In the present paper we have investigated the contribution of protein interactions at this domain to the regulation/function of PKC-δ in neutrophils. Using affinity chromatography we identified actin as a δC2 binding partner in these cells. Fluorescein-labelled δC2, microinjected into immobilized neutrophils, interacts with filamentous actin (F-actin) inside the cell. PKC-δ co-localizes with F-actin in neutrophils, in lamellipodia at the leading edge of the cell. Stimulation with phorbol ester or IgG-opsonized Staphylococcus aureus results in co-ordinated redistribution of PKC-δ and F-actin, and a PKC-δ inhibitor inhibits these changes. Microinjection of δC2 also inhibits F-actin redistribution. Thus PKC-δ binds to F-actin through its C2 domain, and these interactions are important in regulating actin redistribution in neutrophils.
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July 2001
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Research Article|
June 25 2001
Protein kinase C-δ C2-like domain is a binding site for actin and enables actin redistribution in neutrophils
Guillermo LÓPEZ-LLUCH;
Guillermo LÓPEZ-LLUCH
∗Centre for Molecular Medicine, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, U.K.
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Margaret M. BIRD;
Margaret M. BIRD
∗Centre for Molecular Medicine, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, U.K.
†Queen Mary, University of London, Mile End Road, London E1 4NS, U.K.
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Benito CANAS;
Benito CANAS
∗Centre for Molecular Medicine, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, U.K.
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Jasminka GODOVAC-ZIMMERMAN;
Jasminka GODOVAC-ZIMMERMAN
∗Centre for Molecular Medicine, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, U.K.
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Anne RIDLEY;
Anne RIDLEY
‡Ludwig Institute for Cancer Research, 91 Riding House Street, London W1W 7BS, U.K.
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Anthony W. SEGAL;
Anthony W. SEGAL
∗Centre for Molecular Medicine, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, U.K.
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Lodewijk V. DEKKER
Lodewijk V. DEKKER
1
∗Centre for Molecular Medicine, Department of Medicine, University College London, The Rayne Institute, 5 University Street, London WC1E 6JJ, U.K.
1To whom correspondence should be addressed (e-mail rmhalvd@ucl.ac.uk).
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Publisher: Portland Press Ltd
Received:
February 28 2001
Revision Received:
April 04 2001
Accepted:
April 24 2001
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2001
2001
Biochem J (2001) 357 (1): 39–47.
Article history
Received:
February 28 2001
Revision Received:
April 04 2001
Accepted:
April 24 2001
Citation
Guillermo LÓPEZ-LLUCH, Margaret M. BIRD, Benito CANAS, Jasminka GODOVAC-ZIMMERMAN, Anne RIDLEY, Anthony W. SEGAL, Lodewijk V. DEKKER; Protein kinase C-δ C2-like domain is a binding site for actin and enables actin redistribution in neutrophils. Biochem J 1 July 2001; 357 (1): 39–47. doi: https://doi.org/10.1042/bj3570039
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