Source:http://linkedlifedata.com/resource/pubmed/id/11373276
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
30
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| pubmed:dateCreated |
2001-7-23
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| pubmed:abstractText |
Mammalian phospholipase D (PLD) plays a key role in several signal transduction pathways and is involved in many diverse functions. To elucidate the complex molecular regulation of PLD, we investigated PLD-binding proteins obtained from rat brain extract. Here we report that a 43-kDa protein in the rat brain, beta-actin, acts as a major PLD2 direct-binding protein as revealed by peptide mass fingerprinting in combination with matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. We also determined that the region between amino acids 613 and 723 of PLD2 is required for the direct binding of beta-actin, using bacterially expressed glutathione S-transferase fusion proteins of PLD2 fragments. Intriguingly, purified beta-actin potently inhibited both phosphatidylinositol-4,5-bisphosphate- and oleate-dependent PLD2 activities in a concentration-dependent manner (IC50 = 5 nm). In a previous paper, we reported that alpha-actinin inhibited PLD2 activity in an interaction-dependent and an ADP-ribosylation factor 1 (ARF1)-reversible manner (Park, J. B., Kim, J. H., Kim, Y., Ha, S. H., Kim, J. H., Yoo, J.-S., Du, G., Frohman, M. A., Suh, P.-G., and Ryu, S. H. (2000) J. Biol. Chem. 275, 21295-21301). In vitro binding analyses showed that beta-actin could displace alpha-actinin binding to PLD2, demonstrating independent interaction between cytoskeletal proteins and PLD2. Furthermore, ARF1 could steer the PLD2 activity in a positive direction regardless of the inhibitory effect of beta-actin on PLD2. We also observed that beta-actin regulates PLD1 and PLD2 with similar binding and inhibitory potencies. Immunocytochemical and co-immunoprecipitation studies demonstrated the in vivo interaction between the two PLD isozymes and actin in cells. Taken together, these results suggest that the regulation of PLD by cytoskeletal proteins, beta-actin and alpha-actinin, and ARF1 may play an important role in cytoskeleton-related PLD functions.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 4,5-Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
27
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| pubmed:volume |
276
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
28252-60
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11373276-Actins,
pubmed-meshheading:11373276-Animals,
pubmed-meshheading:11373276-Baculoviridae,
pubmed-meshheading:11373276-Brain,
pubmed-meshheading:11373276-COS Cells,
pubmed-meshheading:11373276-Cell Line,
pubmed-meshheading:11373276-Cytoskeleton,
pubmed-meshheading:11373276-DNA, Complementary,
pubmed-meshheading:11373276-Dose-Response Relationship, Drug,
pubmed-meshheading:11373276-Glutathione Transferase,
pubmed-meshheading:11373276-Immunohistochemistry,
pubmed-meshheading:11373276-Inhibitory Concentration 50,
pubmed-meshheading:11373276-Insects,
pubmed-meshheading:11373276-PC12 Cells,
pubmed-meshheading:11373276-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:11373276-Phospholipase D,
pubmed-meshheading:11373276-Precipitin Tests,
pubmed-meshheading:11373276-Protein Binding,
pubmed-meshheading:11373276-Rats,
pubmed-meshheading:11373276-Recombinant Fusion Proteins,
pubmed-meshheading:11373276-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:11373276-Transfection
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| pubmed:year |
2001
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| pubmed:articleTitle |
Actin directly interacts with phospholipase D, inhibiting its activity.
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| pubmed:affiliation |
Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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