βPIX-activated Rac1 stimulates the activation of phospholipase D, which is associated with exocytosis in neuroendocrine cells

Momboisse, Fanny; Lonchamp, Etienne; Calco, Valérie; Ceridono, Mara; Vitale, Nicolas; Bader, Marie‐France; Gasman, Stéphane

doi:10.1242/jcs.038109

Cited by 49 publications

(61 citation statements)

References 55 publications

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“…In the mouse calyx of Held synapse, presynaptic GIT1, or GIT1 together with GIT2, constrains the probability of synaptic vesicle release without altering the readily releasable pool of vesicles; however, GIT2 alone has no significant effect (Montesinos et al, 2015). In adrenal chromaffin cells, neuroendocrine vesicle exocytosis requires both GIT1 and β-PIX, which regulate Arf6 activity to control phospholipase D that promotes vesicle fusion with the membrane (Meyer et al, 2006;Momboisse et al, 2009). β-PIX also contributes to presynaptic function by regulating vesicle targeting (Sun and Bamji, 2011).…”

Section: Functions In the Nervous Systemmentioning

confidence: 99%

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes

Weiyuan

Premont

2016

Journal of Cell Science

130

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The GIT proteins, GIT1 and GIT2, are GTPase-activating proteins (inactivators) for the ADP-ribosylation factor (Arf ) small GTP-binding proteins, and function to limit the activity of Arf proteins. The PIX proteins, α-PIX and β-PIX (also known as ARHGEF6 and ARHGEF7, respectively), are guanine nucleotide exchange factors (activators) for the Rho family small GTP-binding protein family members Rac1 and Cdc42. Through their multi-domain structures, GIT and PIX proteins can also function as signaling scaffolds by binding to numerous protein partners. Importantly, the constitutive association of GIT and PIX proteins into oligomeric GIT-PIX complexes allows these two proteins to function together as subunits of a larger structure that coordinates two distinct small GTP-binding protein pathways and serves as multivalent scaffold for the partners of both constituent subunits. Studies have revealed the involvement of GIT and PIX proteins, and of the GIT-PIX complex, in numerous fundamental cellular processes through a wide variety of mechanisms, pathways and signaling partners. In this Commentary, we discuss recent findings in key physiological systems that exemplify current understanding of the function of this important regulatory complex. Further, we draw attention to gaps in crucial information that remain to be filled to allow a better understanding of the many roles of the GIT-PIX complex in health and disease.

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Section: Functions In the Nervous Systemmentioning

confidence: 99%

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes

Weiyuan

Premont

2016

Journal of Cell Science

130

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“…Phospholipids are also relevant in the modulation of exocytic events. Phosphatidic acid, which is generated following the Rac1-dependent activation of phospholipase D1, has been shown to bind the tSNARE syntaxin 1A and thus strengthens Ca 2+ -induced exocytic responses (Momboisse et al, 2009). The product of its dephosphorylation, diacylglycerol, together with PtdIns(4,5)P 2 , activates MUNC13-1, a regulatory protein that promotes the docking and discharge of neurosecretory vesicles (reviewed by Ory and Gasman, 2011;Martin, 2012).…”

Section: Exocytic Membrane Fusionmentioning

confidence: 99%

Cell surface dynamics – how Rho GTPases orchestrate the interplay between the plasma membrane and the cortical cytoskeleton

Curtis

Meldolesi

2012

Journal of Cell Science

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SummarySmall GTPases are known to regulate hundreds of cell functions. In particular, Rho family GTPases are master regulators of the cytoskeleton. By regulating actin nucleation complexes, Rho GTPases control changes in cell shape, including the extension and/or retraction of surface protrusions and invaginations. Protrusion and invagination of the plasma membrane also involves the interaction between the plasma membrane and the cortical cytoskeleton. This interplay between membranes and the cytoskeleton can lead to an increase or decrease in the plasma membrane surface area and its tension as a result of the fusion (exocytosis) or internalization (endocytosis) of membranous compartments, respectively. For a long time, the cytoskeleton and plasma membrane dynamics were investigated separately. However, studies from many laboratories have now revealed that Rho GTPases, their modulation of the cytoskeleton, and membrane traffic are closely connected during the dynamic remodeling of the cell surface. Arf-and Rab-dependent exocytosis of specific vesicles contributes to the targeting of Rho GTPases and their regulatory factors to discrete sites of the plasma membrane. Rho GTPases regulate the tethering of exocytic vesicles and modulate their subsequent fusion. They also have crucial roles in the different forms of endocytosis, where they participate in the sorting of membrane domains as well as the sculpting and sealing of membrane flasks and cups. Here, we discuss how cell surface dynamics depend on the orchestration of the cytoskeleton and the plasma membrane by Rho GTPases.

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“…In the presence of nonhydrolyzable analogs of GTP, small GTPases Rac1, Cdc42, and RhoA activate PLD1 [26,93,94] and PLD2 [95] in vitro. RhoA [96,97], Rac1 [98], and Cdc42 [99] are PLD1 stimulators in vivo. The C3-exoenzyme from Clostridium botulinum, which inhibits the functioning of Rho proteins via their ADP-ribosylation, decreases the activity of PLD1 [82].…”

Section: +mentioning

confidence: 99%

Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells

Kolesnikov

Nokhrina

Kretynin

et al. 2012

Biochemistry Moscow

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Abbreviations: Gα, α-subunit of heterotrimeric G-protein; PKC, protein kinase C; PLD, phospholipase D; PtdIns(4,5)P 2 , phosphatidylinositol-4,5-bisphosphate. * To whom correspondence should be addressed.Abstract⎯Phospholipase D (PLD) catalyzes hydrolysis of phospholipids with production of phosphatidic acids, which often act as secondary messengers on transmission of intracellular signals. This review summarizes data of various leading laboratories on specific features of organization and regulation of PLD activity in plant and animal cells. The main structural domains of PLD (C2, PX, PH), the active site, and other functionally important parts of the enzyme are considered. Regulatory mechanisms of PLD activity are characterized in detail. Studies associated with molecular design, analysis, and synthesis of new nontoxic substances capable of inhibiting different PLD isoenzymes in vivo are shown to be promising for biotechnology and medicine.

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βPIX-activated Rac1 stimulates the activation of phospholipase D, which is associated with exocytosis in neuroendocrine cells

Cited by 49 publications

References 55 publications

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes

Cell surface dynamics – how Rho GTPases orchestrate the interplay between the plasma membrane and the cortical cytoskeleton

Molecular structure of phospholipase D and regulatory mechanisms of its activity in plant and animal cells

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