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Progr Lipid Res, Available online 28 December 2011 | doi.org/10.1016/j.plipres.2011.12.003 Understanding of the roles of phospholipase D and phosphatidic acid through their binding partners

Abstract

Jin-Hyeok Jang^{a, 1}, Chang Sup Lee^{b, 1, 2}, Daehee Hwang^{a, c}, Sung Ho Ryu*^{a, b, d}

^a School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang, Kyungbook 790-784, South Korea
^b Department of Life Science and Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbook 790-784, South Korea
^c Department of Chemical Engineering, Pohang University of Science and Technology, Pohang, Kyungbook 790-784, South Korea
^d Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang, Kyungbook 790-784, South Korea

^* Corresponding author
¹These authors contributed equally to this work.
²Present address: Beirne B. Carter Center for Immunology Research, University of Virginia, Charlottesville, VA 22908, USA.

Abstract
Phospholipase D (PLD) is a phosphatidyl choline (PC)-hydrolyzing enzyme that generates phosphatidic acid (PA), a lipid second messenger that modulates diverse intracellular signaling. Through interactions with signaling molecules, both PLD and PA can mediate a variety of cellular functions, such as, growth/proliferation, vesicle trafficking, cytoskeleton modulation, development, and morphogenesis. Therefore, systemic approaches for investigating PLD networks including interrelationship between PLD and PA and theirs binding partners, such as proteins and lipids, can enhance fundamental knowledge of roles of PLD and PA in diverse biological processes. In this review, we summarize previously reported protein-protein and protein-lipid interactions of PLD and PA and their binding partners. In addition, we describe the functional roles played by PLD and PA in these interactions, and provide PLD network that summarizes these interactions. The PLD network suggests that PLD and PA could act as a decision maker and/or as a coordinator of signal dynamics. This viewpoint provides a turning point for understanding the roles of PLD-PA as a dynamic signaling hub.

Abbreviations
AMPK, AMP-activated protein kinase; ARF, ADP-ribosylation factor; CDK5, cyclin-dependent kinase 5; CEM, caveolin-enriched membrane; CRMP-2, collapsin response mediator protein-2; EGF, epidermal growth factor; EGFR, EGF receptor; GAP, GTPase-activating protein; GDI, guanine nucleotide dissociation inhibitor; GEF, guanine nucleotide exchange factor; GPCR, G protein-coupled receptor; JAK3, Janus kinase 3; LPA, lysophosphatidic acid; mTOR, mammalian target of rapamycin; mTORC1, mTOR Complex 1; PA, phosphatidic acid; PDE, phosphodiesterase; PDGF, platelet-derived growth factor; PH, pleckstrin homology; PI, phosphoinositides; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate; PI(45)P2, phosphatidylinositol 4,5-bisphosphate; PI(5)P, phosphatidylinositol 5-phosphate; PI4P5K, phosphatidylinositol 4-phosphate 5-kinase; PKC, protein kinase C; PKN, protein kinase N; PLD, phospholipase D; PMA, phorbol ester; PP1cγ, the γ isoform of the protein phosphatase-1 catalytic subunit (PP1cγ); PX, phox homology; RTK, receptor tyrosine kinase

Keywords
Phospholipase D; Phosphatidic acid; Binding partners; Interaction network; Signaling dynamics; Network motif

논문정보

형식Review Paper
게재일2011년 12월 (BRIC 등록일 )
연구진국내 연구진
분야 생명과학 > 세포생물학

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