Coupled Inositide Phosphorylation and Phospholipase D Activation Initiates Clathrin-coat Assembly on Lysosomes

Arneson, Lynne S.; Kunz, Jeannette; Anderson, Richard A.; Traub, Linton M.

doi:10.1074/jbc.274.25.17794

Cited by 103 publications

(80 citation statements)

References 75 publications

(69 reference statements)

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“…More importantly, in mammalian cells, PA can potently stimulate a type I PIPK activity. Quenching PA function with primary alcohols prevents the synthesis of PI(4,5)P 2 and blocks PI(4,5)P 2 -mediated clathrin-coat assembly [36]. This provides a direct evidence for a positive feedback loop between PIPKs and phospholipase D (PLD, the main enzyme to synthesize PA) in mammalian cells.…”

Section: Discussionmentioning

confidence: 76%

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

Lin

et al. 2006

Cell Res

101

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Multiple repeats of membrane occupation and recognition nexus (MORN) motifs were detected in plant phosphatidylinositl monophosphate kinase (PIPK), a key enzyme in PI-signaling pathway. Structural analysis indicates that all the MORN motifs (with varied numbers at ranges of 7-9), which shared high homologies to those of animal ones, were located at N-terminus and sequentially arranged, except those of OsPIPK1 and AtPIPK7, in which the last MORN motif was separated others by an ~100 amino-acid "island" region, revealing the presence of two kinds of MORN arrangements in plant PIPKs. Through employing a yeast-based SMET (sequence of membrane-targeting) system, the MORN motifs were shown being able to target the fusion proteins to cell plasma membrane, which were further confirmed by expression of fused MORN-GFP proteins. Further detailed analysis via deletion studies indicated the MORN motifs in OsPIPK1, together with the 104 amino-acid "island" region are involved in the regulation of differential subcellular localization, i.e. plasma membrane or nucleus, of the fused proteins. Fat Western blot analysis of the recombinant MORN polypeptide, expressed in Escherichia coli, showed that MORN motifs could strongly bind to PA and relatively slightly to PI4P and PI(4,5)P 2 . These results provide informative hints on mechanisms of subcellular localization, as well as regulation of substrate binding, of plant PIPKs.

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Section: Discussionmentioning

confidence: 76%

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

Lin

et al. 2006

Cell Res

101

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“…First, Arf6 has been shown to activate PIP5-kinase and phospholipase D (30,31). Phosphatidic acid, the product of phospholipase D, has been shown to function as a cofactor in the activation of PIP5-kinase (32). PIP5-kinase is responsible for generating PI(4,5)P2, which recruits numerous actin-binding proteins and induces drastic changes in the cortical actin network (33).…”

Section: Discussionmentioning

confidence: 99%

FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex

Ikenouchi

Umeda

2009

Proc. Natl. Acad. Sci. U.S.A.

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The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables during epithelial polarization. However, the mechanisms by which this complex functions are not well elucidated. In the present study, we found that activation of Arf6 is spatiotemporally regulated as a downstream signaling pathway of the Par protein complex. When primordial AJs are formed, Par-3 recruits a scaffolding protein, termed the FERM domain containing 4A (FRMD4A). FRMD4A connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. We propose that the Par-3/FRMD4A/cytohesin-1 complex ensures accurate activation of Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization.

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“…The presence of LAMP-1 suggests that these vesicles are lysosomes or late endosomes, but further characterization will be required for identification. PLD activity has previously been detected in lysosomes (61), but, to our knowledge, the isoform of PLD responsible for this activity has not been defined.…”

Section: Pld1 and Pld2 Exhibit Distinct Differences In Subcellular Lomentioning

confidence: 99%

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

Barton¹,

Bourgoin²,

Kusner

2004

The Journal of Immunology

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Phagocytosis is a fundamental feature of the innate immune system, required for antimicrobial defense, resolution of inflammation, and tissue remodeling. Furthermore, phagocytosis is coupled to a diverse range of cytotoxic effector mechanisms, including the respiratory burst, secretion of inflammatory mediators and Ag presentation. Phospholipase D (PLD) has been linked to the regulation of phagocytosis and subsequent effector responses, but the identity of the PLD isoform(s) involved and the molecular mechanisms of activation are unknown. We used primary human macrophages and human THP-1 promonocytes to characterize the role of PLD in phagocytosis. Macrophages, THP-1 cells, and other human myelomonocytic cells expressed both PLD1 and PLD2 proteins. Phagocytosis of complement-opsonized zymosan was associated with stimulation of the activity of both PLD1 and PLD2, as demonstrated by a novel immunoprecipitation-in vitro PLD assay. Transfection of dominant-negative PLD1 or PLD2 each inhibited the extent of phagocytosis (by 55–65%), and their combined effects were additive (reduction of 91%). PLD1 and PLD2 exhibited distinct localizations in resting macrophages and those undergoing phagocytosis, and only PLD1 localized to the phagosome membrane. The COS-7 monkey fibroblast cell line, which has been used as a heterologous system for the analysis of receptor-mediated phagocytosis, expressed PLD2 but not PLD1. These data support a model in which macrophage phagocytosis is coordinately regulated by both PLD1 and PLD2, with isoform-specific localization. Human myelomonocytic cell lines accurately model PLD-dependent signal transduction events required for phagocytosis, but the heterologous COS cell system does not.

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Coupled Inositide Phosphorylation and Phospholipase D Activation Initiates Clathrin-coat Assembly on Lysosomes

Cited by 103 publications

References 75 publications

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

MORN motifs in plant PIPKs are involved in the regulation of subcellular localization and phospholipid binding

FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex

Phospholipases D1 and D2 Coordinately Regulate Macrophage Phagocytosis

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