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

doi:10.1016/S0014-5793(98)00661-9

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 journal › Article › peer-review

18 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 language	English
Pages (from-to)	231-235
Number of pages	5
Journal	FEBS Letters
Volume	430
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(98)00661-9
Publication status	Published - 1998 Jul 3

Bibliographical note

Funding Information:
This work is supported in part by the program of the Ministry of Education (BSRI-97-4434) and by the `1997 Good Health R&D Project' of the Ministry of Health and Welfare from the Republic of Korea.

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(98)00661-9

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title = "Activation of phospholipase D1 by direct interaction with ADP- ribosylation factor 1 and Ra1A",

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.",

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

note = "Funding Information: This work is supported in part by the program of the Ministry of Education (BSRI-97-4434) and by the `1997 Good Health R&D Project' of the Ministry of Health and Welfare from the Republic of Korea.",

year = "1998",

month = jul,

day = "3",

doi = "10.1016/S0014-5793(98)00661-9",

language = "English",

volume = "430",

pages = "231--235",

journal = "FEBS Letters",

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TY - JOUR

T1 - Activation of phospholipase D1 by direct interaction with ADP- ribosylation factor 1 and Ra1A

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

N1 - Funding Information: This work is supported in part by the program of the Ministry of Education (BSRI-97-4434) and by the `1997 Good Health R&D Project' of the Ministry of Health and Welfare from the Republic of Korea.

PY - 1998/7/3

Y1 - 1998/7/3

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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DO - 10.1016/S0014-5793(98)00661-9

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AN - SCOPUS:0032479476

SN - 0014-5793

VL - 430

SP - 231

EP - 235

JO - FEBS Letters

JF - FEBS Letters

IS - 3

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

Abstract

Bibliographical note

All Science Journal Classification (ASJC) codes

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