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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Actin directly interacts with phospholipase D, inhibiting its activity

Cited 88 times inthomson ciCited 88 times inthomson ci
Title
Actin directly interacts with phospholipase D, inhibiting its activity
Author
Lee, SukmookPark, Jong BaeKim, Jong HyunKim, YongKim, Jung HwanShin, Kum-JooLee, Jun SungHa, Sang HoonSuh, Pann-GhillRyu, Sung Ho
Issue Date
2001-07
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.276, no.30, pp.28252 - 28260
Abstract
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 phosphaticlylinositol-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., Sub, 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 a-actinin, and ARF1 may play an important role in cytoskeleton-related PLD functions
URI
https://scholarworks.unist.ac.kr/handle/201301/16523
URL
http://www.jbc.org/content/276/30/28252.long
DOI
10.1074/jbc.M008521200
ISSN
0021-9258
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BIO_Journal Papers
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