The regulation of phospholipase D by inosital phospholipids and small GTPases

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The regulation of phospholipase D by inosital phospholipids and small GTPases. / Powner, Dale; Wakelam, Michael.

In: FEBS Letters, Vol. 531, No. 1, 01.10.2002, p. 62-64.

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@article{95d6cfb2694c4d47ad8e3e11d92e6bff,
title = "The regulation of phospholipase D by inosital phospholipids and small GTPases",
abstract = "Phospholipase D1 and D2 (PLD1, PLD2) both have PX and PH domains in their N-terminal regions with these inositol lipid binding domains playing key roles in regulating PLD activity and localisation. The activity of PLD1 is also regulated by protein kinase C and members of the Rho and Arf families of GTPases. Each of these proteins binds to unique sites; however, there appears to be little in vitro discrimination between individual family members. In agonist-stimulated cells, however, there is specificity, with, for example in RBL-2H3 cells, antigen stimulating the activation of PLD1 by association with Arf6, Rac1 and protein kinase Calpha. PLD2 appears to be less directly regulated by GTPases and rather is primarily controlled through interaction with phosphatidylinositol 4-phosphate 5-kinase that generates the activating phosphatidylinositol, 4,5-bisphosphate. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.",
keywords = "Rac1, phospholipase D, phosphatidylinositol 4-phosphate 5-kinase, phosphatidylinositol 4,5-bisphosphate, Arf6",
author = "Dale Powner and Michael Wakelam",
year = "2002",
month = oct,
day = "1",
doi = "10.1016/S0014-5793(02)03410-5",
language = "English",
volume = "531",
pages = "62--64",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - The regulation of phospholipase D by inosital phospholipids and small GTPases

AU - Powner, Dale

AU - Wakelam, Michael

PY - 2002/10/1

Y1 - 2002/10/1

N2 - Phospholipase D1 and D2 (PLD1, PLD2) both have PX and PH domains in their N-terminal regions with these inositol lipid binding domains playing key roles in regulating PLD activity and localisation. The activity of PLD1 is also regulated by protein kinase C and members of the Rho and Arf families of GTPases. Each of these proteins binds to unique sites; however, there appears to be little in vitro discrimination between individual family members. In agonist-stimulated cells, however, there is specificity, with, for example in RBL-2H3 cells, antigen stimulating the activation of PLD1 by association with Arf6, Rac1 and protein kinase Calpha. PLD2 appears to be less directly regulated by GTPases and rather is primarily controlled through interaction with phosphatidylinositol 4-phosphate 5-kinase that generates the activating phosphatidylinositol, 4,5-bisphosphate. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

AB - Phospholipase D1 and D2 (PLD1, PLD2) both have PX and PH domains in their N-terminal regions with these inositol lipid binding domains playing key roles in regulating PLD activity and localisation. The activity of PLD1 is also regulated by protein kinase C and members of the Rho and Arf families of GTPases. Each of these proteins binds to unique sites; however, there appears to be little in vitro discrimination between individual family members. In agonist-stimulated cells, however, there is specificity, with, for example in RBL-2H3 cells, antigen stimulating the activation of PLD1 by association with Arf6, Rac1 and protein kinase Calpha. PLD2 appears to be less directly regulated by GTPases and rather is primarily controlled through interaction with phosphatidylinositol 4-phosphate 5-kinase that generates the activating phosphatidylinositol, 4,5-bisphosphate. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

KW - Rac1

KW - phospholipase D

KW - phosphatidylinositol 4-phosphate 5-kinase

KW - phosphatidylinositol 4,5-bisphosphate

KW - Arf6

UR - http://www.scopus.com/inward/record.url?scp=0037201953&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(02)03410-5

DO - 10.1016/S0014-5793(02)03410-5

M3 - Article

C2 - 12401204

VL - 531

SP - 62

EP - 64

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -