Regulation of phospholipase D2 by GTP-dependent interaction with dynamin

Jong Bae Park; Chang Sup Lee; Hye Young Lee; Il Shin Kim; Byoung Dae Lee; Il Ho Jang; Yon Woo Jung; Yong Seok Oh; Mi Young Han; Ole Norregaard Jensen; Peter Roepstorff; Pann Ghill Suh; Sung Ho Ryu

doi:10.1016/j.advenzreg.2003.11.021

Regulation of phospholipase D2 by GTP-dependent interaction with dynamin

Jong Bae Park, Chang Sup Lee, Hye Young Lee, Il Shin Kim, Byoung Dae Lee, Il Ho Jang, Yon Woo Jung, Yong Seok Oh, Mi Young Han, Ole Norregaard Jensen, Peter Roepstorff, Pann Ghill Suh, Sung Ho Ryu

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Phospholipase D (PLD) has been implicated in various cellular events such as vesicle trafficking, cytoskeletal rearrangement, and neurotransmitter release. However, the functional significance of PLD in these processes is still unclear. In this study, we identified dynamin as a PLD2-interacting molecule in rat brain. Dynamin is a GTPase family member and has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. Dynamin was found to interact with PLD2 in a GTP-dependent manner, whereas DYN-K44A, a dominant negative mutant of dynamin, did not interact with PLD2. Interaction between dynamin and PLD2 was transient after treatment with EGF, and this was found to correlate with the activation of PLD2. Furthermore, overexpression of the DYN-K44A repressed the EGF induced PLD activity and their interaction in the COS-7 cells. These results suggest that the GTP-dependent interaction of PLD2 and dynamin might play an important role in the EGF-induced PLD activation.

Original language	English (US)
Pages (from-to)	249-264
Number of pages	16
Journal	Advances in Enzyme Regulation
Volume	44
Issue number	1
DOIs	https://doi.org/10.1016/j.advenzreg.2003.11.021
State	Published - 2004
Externally published	Yes

Keywords

DG, diacylglycerol
LPA, lysophosphatidic acid
PA, phosphatidic acid
PC, phosphatidylcholine
PKC, protein kinase C (EC 2.7.1.37)
PLC, phospholipase C (EC 3.1.4.11)
PLD, phospholipase D (EC 3.1.4.4)

ASJC Scopus subject areas

Molecular Medicine
Molecular Biology
Genetics
Cancer Research

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10.1016/j.advenzreg.2003.11.021

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@article{3b8b820ab80043ac9c7ec66dee2be1b2,

title = "Regulation of phospholipase D2 by GTP-dependent interaction with dynamin",

abstract = "Phospholipase D (PLD) has been implicated in various cellular events such as vesicle trafficking, cytoskeletal rearrangement, and neurotransmitter release. However, the functional significance of PLD in these processes is still unclear. In this study, we identified dynamin as a PLD2-interacting molecule in rat brain. Dynamin is a GTPase family member and has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. Dynamin was found to interact with PLD2 in a GTP-dependent manner, whereas DYN-K44A, a dominant negative mutant of dynamin, did not interact with PLD2. Interaction between dynamin and PLD2 was transient after treatment with EGF, and this was found to correlate with the activation of PLD2. Furthermore, overexpression of the DYN-K44A repressed the EGF induced PLD activity and their interaction in the COS-7 cells. These results suggest that the GTP-dependent interaction of PLD2 and dynamin might play an important role in the EGF-induced PLD activation.",

keywords = "DG, diacylglycerol, LPA, lysophosphatidic acid, PA, phosphatidic acid, PC, phosphatidylcholine, PKC, protein kinase C (EC 2.7.1.37), PLC, phospholipase C (EC 3.1.4.11), PLD, phospholipase D (EC 3.1.4.4)",

author = "Park, {Jong Bae} and Lee, {Chang Sup} and Lee, {Hye Young} and Kim, {Il Shin} and Lee, {Byoung Dae} and Jang, {Il Ho} and Jung, {Yon Woo} and Oh, {Yong Seok} and Han, {Mi Young} and Jensen, {Ole Norregaard} and Peter Roepstorff and Suh, {Pann Ghill} and Ryu, {Sung Ho}",

note = "Funding Information: This work was supported in part by the grant of the 21st Frontier Functional Proteomics Research (FPR03A5-43-100) and the National Research Laboratory of the Ministry of Science and Technology (2000-N-NL-01-C-040) in the Republic of Korea.",

year = "2004",

doi = "10.1016/j.advenzreg.2003.11.021",

language = "English (US)",

volume = "44",

pages = "249--264",

journal = "Advances in Enzyme Regulation",

issn = "0065-2571",

publisher = "Elsevier Ltd",

number = "1",

}

TY - JOUR

T1 - Regulation of phospholipase D2 by GTP-dependent interaction with dynamin

AU - Park, Jong Bae

AU - Lee, Chang Sup

AU - Lee, Hye Young

AU - Kim, Il Shin

AU - Lee, Byoung Dae

AU - Jang, Il Ho

AU - Jung, Yon Woo

AU - Oh, Yong Seok

AU - Han, Mi Young

AU - Jensen, Ole Norregaard

AU - Roepstorff, Peter

AU - Suh, Pann Ghill

AU - Ryu, Sung Ho

N1 - Funding Information: This work was supported in part by the grant of the 21st Frontier Functional Proteomics Research (FPR03A5-43-100) and the National Research Laboratory of the Ministry of Science and Technology (2000-N-NL-01-C-040) in the Republic of Korea.

PY - 2004

Y1 - 2004

N2 - Phospholipase D (PLD) has been implicated in various cellular events such as vesicle trafficking, cytoskeletal rearrangement, and neurotransmitter release. However, the functional significance of PLD in these processes is still unclear. In this study, we identified dynamin as a PLD2-interacting molecule in rat brain. Dynamin is a GTPase family member and has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. Dynamin was found to interact with PLD2 in a GTP-dependent manner, whereas DYN-K44A, a dominant negative mutant of dynamin, did not interact with PLD2. Interaction between dynamin and PLD2 was transient after treatment with EGF, and this was found to correlate with the activation of PLD2. Furthermore, overexpression of the DYN-K44A repressed the EGF induced PLD activity and their interaction in the COS-7 cells. These results suggest that the GTP-dependent interaction of PLD2 and dynamin might play an important role in the EGF-induced PLD activation.

AB - Phospholipase D (PLD) has been implicated in various cellular events such as vesicle trafficking, cytoskeletal rearrangement, and neurotransmitter release. However, the functional significance of PLD in these processes is still unclear. In this study, we identified dynamin as a PLD2-interacting molecule in rat brain. Dynamin is a GTPase family member and has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. Dynamin was found to interact with PLD2 in a GTP-dependent manner, whereas DYN-K44A, a dominant negative mutant of dynamin, did not interact with PLD2. Interaction between dynamin and PLD2 was transient after treatment with EGF, and this was found to correlate with the activation of PLD2. Furthermore, overexpression of the DYN-K44A repressed the EGF induced PLD activity and their interaction in the COS-7 cells. These results suggest that the GTP-dependent interaction of PLD2 and dynamin might play an important role in the EGF-induced PLD activation.

KW - DG, diacylglycerol

KW - LPA, lysophosphatidic acid

KW - PA, phosphatidic acid

KW - PC, phosphatidylcholine

KW - PKC, protein kinase C (EC 2.7.1.37)

KW - PLC, phospholipase C (EC 3.1.4.11)

KW - PLD, phospholipase D (EC 3.1.4.4)

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U2 - 10.1016/j.advenzreg.2003.11.021

DO - 10.1016/j.advenzreg.2003.11.021

M3 - Article

C2 - 15581494

AN - SCOPUS:9644310488

SN - 0065-2571

VL - 44

SP - 249

EP - 264

JO - Advances in Enzyme Regulation

JF - Advances in Enzyme Regulation

IS - 1

ER -

Regulation of phospholipase D2 by GTP-dependent interaction with dynamin

Abstract

Keywords

ASJC Scopus subject areas

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