Binding of Cdc42 to phospholipase D1 is important in neurite outgrowth of neural stem cells

Yoon, Mee-Sup; Cho, Chan Ho; Lee, Ki Sung; Han, Joong‐Soo

doi:10.1016/j.bbrc.2006.06.111

Cited by 11 publications

(8 citation statements)

References 27 publications

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“…We previously reported that PLD1 is involved in various neuronal signaling pathways and is an important regulator of neuron function (Yoon et al., 2006, Yoon et al., 2012). We also showed that HPCA increased the activity and expression of PLD in various cell types (Hyun et al., 2000, Oh et al., 2006).…”

Section: Resultsmentioning

confidence: 99%

Hippocalcin Promotes Neuronal Differentiation and Inhibits Astrocytic Differentiation in Neural Stem Cells

et al. 2017

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SummaryHippocalcin (HPCA) is a calcium-binding protein that is restricted to nervous tissue and contributes to neuronal activity. Here we report that, in addition to inducing neurogenesis, HPCA inhibits astrocytic differentiation of neural stem cells. It promotes neurogenesis by regulating protein kinase Cα (PKCα) activation by translocating to the membrane and binding to phosphoinositide-dependent protein kinase 1 (PDK1), which induces PKCα phosphorylation. We also found that phospholipase D1 (PLD1) is implicated in the HPCA-mediated neurogenesis pathway; this enzyme promotes dephosphorylation of signal transducer and activator of transcription 3 (STAT3[Y705]), which is necessary for astrocytic differentiation. Moreover, we found that the SH2-domain-containing tyrosine phosphatase 1 (SHP-1) acts upstream of STAT3. Importantly, this SHP-1-dependent STAT3-inhibitory mechanism is closely involved in neurogenesis and suppression of gliogenesis by HPCA. Taken together, these observations suggest that HPCA promotes neuronal differentiation through activation of the PKCα/PLD1 cascade followed by activation of SHP-1, which dephosphorylates STAT3(Y705), leading to inhibition of astrocytic differentiation.

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Section: Resultsmentioning

confidence: 99%

Hippocalcin Promotes Neuronal Differentiation and Inhibits Astrocytic Differentiation in Neural Stem Cells

et al. 2017

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“…PIP 3 interacts with this domain and stimulates activity of PLD1 [55]. PLD binds to other proteins: PLCγ1 [56], Grb2 and Sos [57-59], cdc42 [60], Syk [61] and PIP-Kinase [62]. …”

Section: Introductionmentioning

confidence: 99%

The exquisite regulation of PLD2 by a wealth of interacting proteins: S6K, Grb2, Sos, WASp and Rac2 (And a surprise discovery: PLD2 is a GEF)

Gómez‐Cambronero

2011

Cellular Signalling

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PLD catalyzes the conversion of the membrane phospholipid phosphatidylcholine to choline and phosphatidic acid (PA). PLD's mission in the cell is two-fold: phospholipid turnover with maintenance of the structural integrity of cellular/intracellular membranes and cell signaling through PA and its metabolites. Precisely, through its product of the reaction, PA, PLD has been implicated in a variety of physiological cellular functions, such as intracellular protein trafficking, cytoskeletal dynamics, chemotaxis of leukocytes and cell proliferation. The catalytic (HKD) and regulatory (PH and PX) domains were studied in detail in the PLD1 isoform, but PLD2 was traditionally studied in lesser detail and much less was known about its regulation. Our laboratory has been focusing on the study of PLD2 regulation in mammalian cells. Over the past few years, we have reported, in regards to the catalytic action of PLD, that PA is a chemoattractant agent that binds to and signals inside the cell through the ribosomal S6 kinases (S6K). Regarding the regulatory domains of PLD2, we have reported the discovery of the PLD2 interaction with Grb2 via Y169 in the PX domain, and further association to Sos, which results in an increase of de novo DNA synthesis and an interaction (also with Grb2) via the adjacent residue Y179, leading to the regulation of cell ruffling, chemotaxis and phagocytosis of leukocytes. We also review the complex regulation by tyrosine phosphorylation by epidermal growth factor receptor (EGF-R), Janus Kinase 3 (JAK3) and Src and the role of phosphatases. Recently, there is evidence supporting a new level of regulation of PLD2 at the PH domain, by the discovery of CRIB domains and a Rac2-PLD2 interaction that leads to a dual (positive and negative) effect on its enzymatic activity. Lastly, we review the surprising finding of PLD2 acting as a GEF. A phospholipase such as PLD that exists already in the cell membrane that acts directly on Rac allows a quick response of the cell without intermediary signaling molecules. This provides only the latest level of PLD2 regulation in a field that promises newer and exciting advances in the next few years.

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“…PLD1 activity is regulated particularly by interactions with small GTPases that belong to the ARF and Rho families (Powner and Wakelam 2002 ; Rudge and Wakelam 2009 ). The transfection of RhoA, Cdc42, or Rac1 can activate PLD1 (Powner and Wakelam 2002 ; Yoon et al 2006 ), which has been implicated in the regulation of the actin cytoskeleton (Rudge and Wakelam 2009 ). PLD1 controls many physiological functions, such as cell migration and neuronal axon formation, via this regulatory action.…”

Section: Role Of Pld1 In Neuronal Differentiation Of Nscsmentioning

confidence: 99%

“…PLD1 controls many physiological functions, such as cell migration and neuronal axon formation, via this regulatory action. In NSCs, the expression levels of Cdc42 and RhoA were increased during neuronal differentiation, and PLD1 and Cdc42 were co-localized in neurites, while RhoA was localized in the cytosol (Yoon et al 2006 ). Further, Cdc42 was bound to PLD1 during differentiation, and dominant-negative Cdc42 (Cdc42N17) decreased PLD activity and neurite outgrowth.…”

Section: Role Of Pld1 In Neuronal Differentiation Of Nscsmentioning

confidence: 99%

“…PLD1 is expressed in many functionally diverse brain areas, including the cerebral cortex, hippocampus, brain stem, spinal cord, and olfactory bulb (Lee et al 2000 ). Recent studies have reported that the signal-dependent activation of PLD1 is important for neuronal differentiation in NSCs (Park et al 2015 , 2017 ; Yoon et al 2005 , 2006 ). PLD2 is almost exclusively found in the light membrane “lipid raft” fraction of the plasma membrane (Gomez-Cambronero and Keire 1998 ).…”

Section: Introductionmentioning

confidence: 99%

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Phospholipase D1 Signaling: Essential Roles in Neural Stem Cell Differentiation

Park

Han

2018

J Mol Neurosci

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Phospholipase D1 (PLD1) is generally accepted as playing an important role in the regulation of multiple cell functions, such as cell growth, survival, differentiation, membrane trafficking, and cytoskeletal organization. Recent findings suggest that PLD1 also plays an important role in the regulation of neuronal differentiation of neuronal cells. Moreover, PLD1-mediated signaling molecules dynamically regulate the neuronal differentiation of neural stem cells (NSCs). Rho family GTPases and Ca2+-dependent signaling, in particular, are closely involved in PLD1-mediated neuronal differentiation of NSCs. Moreover, PLD1 has a significant effect on the neurogenesis of NSCs via the regulation of SHP-1/STAT3 activation. Therefore, PLD1 has now attracted significant attention as an essential neuronal signaling molecule in the nervous system. In the current review, we summarize recent findings on the regulation of PLD1 in neuronal differentiation and discuss the potential role of PLD1 in the neurogenesis of NSCs.

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Binding of Cdc42 to phospholipase D1 is important in neurite outgrowth of neural stem cells

Cited by 11 publications

References 27 publications

Hippocalcin Promotes Neuronal Differentiation and Inhibits Astrocytic Differentiation in Neural Stem Cells

Hippocalcin Promotes Neuronal Differentiation and Inhibits Astrocytic Differentiation in Neural Stem Cells

The exquisite regulation of PLD2 by a wealth of interacting proteins: S6K, Grb2, Sos, WASp and Rac2 (And a surprise discovery: PLD2 is a GEF)

Phospholipase D1 Signaling: Essential Roles in Neural Stem Cell Differentiation

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