Phospholipase D Is Involved in Myogenic Differentiation through Remodeling of Actin Cytoskeleton

Komati, Hiba; Naro, Fabio; Mébarek, Saida; Arcangelis, Vania De; Adamo, Sergio; Lagarde, Michel; Prigent, Annie‐France; Némoz, Georges

doi:10.1091/mbc.e04-06-0459

Cited by 71 publications

(81 citation statements)

References 61 publications

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“…Several lines of evidence support our hypothesis. First, RhoA can interact with PLD1 when they are coexpressed in N2a cells, which is consistent with previous studies Bae et al, 1998;Yamazaki et al, 1999, Du et al, 2000Komati et al, 2005;Yoon et al, 2005;Gayral et al, 2006). Second, the reduction of dendritic branching caused by active RhoA can be partially rescued by PLD1 siRNA.…”

Section: Discussionsupporting

confidence: 91%

“…Recent studies have suggested that RhoA directly interacts with and activates PLD1 both in vitro and in vivo Bae et al, 1998;Yamazaki et al, 1999;Du et al, 2000;Komati et al, 2005;Yoon et al, 2005;Gayral et al, 2006). In this study, we showed that PLD1 has the same effects as RhoA in reducing the number of dendritic branches.…”

Section: Pld1 Acts As Downstream Target Of Rhoa To Suppress Dendriticsupporting

confidence: 64%

“…In the present study, we focused on PLD1 because it can be directly activated by RhoA both in vitro and in vivo Bae et al, 1998;Yamazaki et al, 1999;Du et al, 2000;Komati et al, 2005;Yoon et al, 2005;Gayral et al, 2006). Using cultured hippocampal neurons as a cellular model, we found that PLD1 negatively regulated dendritic branching.…”

Section: Introductionmentioning

confidence: 94%

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PLD1 Negatively Regulates Dendritic Branching

Zhu

Kang

Zhang

et al. 2012

Journal of Neuroscience

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Neurons have characteristic dendritic arborization patterns that contribute to information processing. One essential component of dendritic arborization is the formation of a specific number of branches. Although intracellular pathways promoting dendritic growth and branching are being elucidated, the mechanisms that negatively regulate the branching of dendrites remain enigmatic. In this study, using gain-of-function and loss-of-function studies, we show that phospholipase D1 (PLD1) acts as a negative regulator of dendritic branching in cultured hippocampal neurons from embryonic day 18 rat embryos. Overexpression of wild-type PLD1 (WT-PLD1) decreases the complexity of dendrites, whereas knockdown or inhibition of PLD1 increases dendritic branching. We further demonstrated that PLD1 acts downstream of RhoA, one of the small Rho GTPases, to suppress dendritic branching. The restriction of dendritic branching by constitutively active RhoA (V14-RhoA) can be partially rescued by knockdown of PLD1. Moreover, the inhibition of dendritic branching by V14-RhoA and WT-PLD1 can be partially ameliorated by reducing the level of phosphatidic acid (PA), which is the enzymatic product of PLD1. Together, these results suggest that RhoA-PLD1-PA may represent a novel signaling pathway in the restriction of dendritic branching and may thus provide insight into the mechanisms of dendritic morphogenesis.

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Section: Discussionsupporting

confidence: 91%

Section: Pld1 Acts As Downstream Target Of Rhoa To Suppress Dendriticsupporting

confidence: 64%

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PLD1 Negatively Regulates Dendritic Branching

Zhu

Kang

Zhang

et al. 2012

Journal of Neuroscience

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“…C2C12 differentiation is markedly inhibited by 1-butanol, an inhibitor of the PLD-catalyzed transphosphatidylation reaction, and also by the knockdown of PLD1, but not PLD2. Further cytoskeleton (Komati et al, 2005). Notably, a potential role of PLD in the autocrine regulation of satellite cell differentiation upon growth factor withdrawal has not been examined, and whether, and how, PLD is involved in mTOR signaling in myogenic differentiation is not known.…”

Section: Introductionmentioning

confidence: 99%

PLD regulates myoblast differentiation through the mTOR-IGF2 pathway

Yoon

Chen

2008

Journal of Cell Science

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investigation has revealed that PLD1 is unlikely to regulate myogenesis through modulation of the actin cytoskeleton as previously suggested. Instead, PLD1 positively regulates mTOR signaling leading to the production of IGF2, an autocrine factor instrumental for the initiation of satellite cell differentiation. Furthermore, exogenous IGF2 fully rescues the differentiation defect resulting from PLD1 knockdown. Hence, PLD1 is critically involved in skeletal myogenesis by regulating the mTOR-IGF2 pathway. Key words: mTOR, Myogenesis, Phospholipase D (PLD) Summary PLD regulates myoblast differentiation through the

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“…There is also evidence that PLD interacts directly with the actin cytoskeleton. Komati et al (39) showed that PLD regulates myogenesis by inducing PA-dependent actin fiber formation. Roach et al (34) showed that PA regulates actin cytoskeletal reorganization by controlling the localization and function of PIPKI, an enzyme that produces the key actin cytoskeleton-regulating lipid, PI(4,5)P2.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidic Acid Produced by RalA-activated PLD2 Stimulates Caveolae-mediated Endocytosis and Trafficking in Endothelial Cells

Jiang

Sverdlov²,

Tóth³

et al. 2016

Journal of Biological Chemistry

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Caveolae are the primary route for internalization and transendothelial transport of macromolecules, such as insulin and albumin. Caveolae-mediated endocytosis is activated by Src-dependent caveolin-1 (Cav-1) phosphorylation and subsequent recruitment of dynamin-2 and filamin A (FilA), which facilitate vesicle fission and trafficking, respectively. Here, we tested the role of RalA and phospholipase D (PLD) signaling in the regulation of caveolae-mediated endocytosis and trafficking. The addition of albumin to human lung microvascular endothelial cells induced the activation of RalA within minutes, and siRNAmediated down-regulation of RalA abolished fluorescent BSA uptake. Co-immunoprecipitation studies revealed that albumin induced the association between RalA, Cav-1, and FilA; however, RalA knockdown with siRNA did not affect FilA recruitment to Cav-1, suggesting that RalA was not required for FilA and Cav-1 complex formation. Rather, RalA probably facilitates caveolae-mediated endocytosis by activating downstream effectors. PLD2 was shown to be activated by RalA, and inhibition of PLD2 abolished Alexa-488-BSA uptake, indicating that phosphatidic acid (PA) generated by PLD2 may facilitate caveolaemediated endocytosis. Furthermore, using a PA biosensor, GFP-PASS, we observed that BSA induced an increase in PA co-localization with Cav-1-RFP, which could be blocked by a dominant negative PLD2 mutant. Total internal reflection fluorescence microscopy studies of Cav-1-RFP also showed that fusion of caveolae with the basal plasma membrane was dependent on PLD2 activity. Thus, our results suggest that the small GTPase RalA plays an important role in promoting invagination and trafficking of caveolae, not by potentiating the association between Cav-1 and FilA but by stimulating PLD2-mediated generation of phosphatidic acid.Caveolae-mediated transcellular transport of macromolecules through endothelial cells (ECs) 2 lining blood vessels is a highly selective and regulated process (1). Although the signaling mechanisms regulating the invagination and internalization (endocytosis) of caveolae have not been fully characterized, it was shown that Src-dependent phosphorylation of the large GTPase dynamin-2 (2, 3) and its recruitment to the neck of caveolae (4), phosphorylation of caveolin-1 Tyr-14 (5) and subsequent recruitment of actin cross-linking protein filamin A (FilA) to caveolae (6), and dynamic actin remodeling (7) are some of the general requirements (8).In addition to the large GTPase dynamin-2, which is required for fission of caveolae from the plasma membrane, several small GTPases detected in caveolin-enriched membrane fractions have been proposed to participate in caveolae-mediated transport. For example, Cdc42, a small GTPase of the Rho family, was detected in caveolae (9), where it is thought to control caveolae-mediated endocytosis by regulating actin polymerization and interactions between the actin cytoskeleton and intersectin, a scaffolding protein required for efficient fission and internalization of ...

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Phospholipase D Is Involved in Myogenic Differentiation through Remodeling of Actin Cytoskeleton

Cited by 71 publications

References 61 publications

PLD1 Negatively Regulates Dendritic Branching

PLD1 Negatively Regulates Dendritic Branching

PLD regulates myoblast differentiation through the mTOR-IGF2 pathway

Phosphatidic Acid Produced by RalA-activated PLD2 Stimulates Caveolae-mediated Endocytosis and Trafficking in Endothelial Cells

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