Activation of phospholipase D1 by direct interaction with ADP- ribosylation factor 1 and Ra1A

Jae Ho Kim, Sang Do Lee, Jung Min Han, Taehoon G. Lee, Yong Kim, Jong Bae Park, J. David Lambeth, Pann Ghill Suh, Sung Ho Ryu

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

Abstract Phospholipase D1 (PLD1) is known to be activated by ADP- ribosylation factor 1 (ARF1). We report here that ARF1 co-immunoprecipitates with PLD1 and that the ARF1-dependent PLD activation is induced by the direct interaction between ARF1 and PLD1. We found that Ra1A, another member of the small GTP-binding proteins, synergistically enhances the ARF1-dependent PLD activity with an EC50 of about 30 nM. Using in vitro binding assay, we show that ARF1 and Ra1A directly interact with different sites of PLD1. The results suggest that the independent interactions of Ra1A and ARF1 with PLD1 are responsible for the synergistic activation.

Original languageEnglish
Pages (from-to)231-235
Number of pages5
JournalFEBS Letters
Volume430
Issue number3
DOIs
Publication statusPublished - 1998 Jul 3

Fingerprint

ADP-Ribosylation Factor 1
Chemical activation
phospholipase D1
GTP-Binding Proteins
Assays

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Kim, Jae Ho ; Lee, Sang Do ; Han, Jung Min ; Lee, Taehoon G. ; Kim, Yong ; Park, Jong Bae ; Lambeth, J. David ; Suh, Pann Ghill ; Ryu, Sung Ho. / Activation of phospholipase D1 by direct interaction with ADP- ribosylation factor 1 and Ra1A. In: FEBS Letters. 1998 ; Vol. 430, No. 3. pp. 231-235.
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abstract = "Abstract Phospholipase D1 (PLD1) is known to be activated by ADP- ribosylation factor 1 (ARF1). We report here that ARF1 co-immunoprecipitates with PLD1 and that the ARF1-dependent PLD activation is induced by the direct interaction between ARF1 and PLD1. We found that Ra1A, another member of the small GTP-binding proteins, synergistically enhances the ARF1-dependent PLD activity with an EC50 of about 30 nM. Using in vitro binding assay, we show that ARF1 and Ra1A directly interact with different sites of PLD1. The results suggest that the independent interactions of Ra1A and ARF1 with PLD1 are responsible for the synergistic activation.",
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Kim, JH, Lee, SD, Han, JM, Lee, TG, Kim, Y, Park, JB, Lambeth, JD, Suh, PG & Ryu, SH 1998, 'Activation of phospholipase D1 by direct interaction with ADP- ribosylation factor 1 and Ra1A', FEBS Letters, vol. 430, no. 3, pp. 231-235. https://doi.org/10.1016/S0014-5793(98)00661-9

Activation of phospholipase D1 by direct interaction with ADP- ribosylation factor 1 and Ra1A. / Kim, Jae Ho; Lee, Sang Do; Han, Jung Min; Lee, Taehoon G.; Kim, Yong; Park, Jong Bae; Lambeth, J. David; Suh, Pann Ghill; Ryu, Sung Ho.

In: FEBS Letters, Vol. 430, No. 3, 03.07.1998, p. 231-235.

Research output: Contribution to journalArticle

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AU - Kim, Jae Ho

AU - Lee, Sang Do

AU - Han, Jung Min

AU - Lee, Taehoon G.

AU - Kim, Yong

AU - Park, Jong Bae

AU - Lambeth, J. David

AU - Suh, Pann Ghill

AU - Ryu, Sung Ho

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N2 - Abstract Phospholipase D1 (PLD1) is known to be activated by ADP- ribosylation factor 1 (ARF1). We report here that ARF1 co-immunoprecipitates with PLD1 and that the ARF1-dependent PLD activation is induced by the direct interaction between ARF1 and PLD1. We found that Ra1A, another member of the small GTP-binding proteins, synergistically enhances the ARF1-dependent PLD activity with an EC50 of about 30 nM. Using in vitro binding assay, we show that ARF1 and Ra1A directly interact with different sites of PLD1. The results suggest that the independent interactions of Ra1A and ARF1 with PLD1 are responsible for the synergistic activation.

AB - Abstract Phospholipase D1 (PLD1) is known to be activated by ADP- ribosylation factor 1 (ARF1). We report here that ARF1 co-immunoprecipitates with PLD1 and that the ARF1-dependent PLD activation is induced by the direct interaction between ARF1 and PLD1. We found that Ra1A, another member of the small GTP-binding proteins, synergistically enhances the ARF1-dependent PLD activity with an EC50 of about 30 nM. Using in vitro binding assay, we show that ARF1 and Ra1A directly interact with different sites of PLD1. The results suggest that the independent interactions of Ra1A and ARF1 with PLD1 are responsible for the synergistic activation.

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