Wiring of the brain by a range of guidance cues

Yamamoto, Naoya; Tamada, Atsushi; Murakami, Fujio

doi:10.1016/s0301-0082(02)00129-6

Cited by 61 publications

(49 citation statements)

References 139 publications

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“…S3). Enriched motifs associated with mouse brain development included: (1) proline at the ϩ1 position after the phosphorylation site (p ϩ 1) combined with lysine at p ϩ 3, p ϩ 4 or p ϩ 5; (2) arginine at P-2 or P-3; and (3) aspartic acid and glutamic acid at p ϩ 2. These results indicated that the strategy is able to enrich for both acidic and basic phosphopeptides.…”

Section: Identification and Quantification Of Phosphopeptides And Formentioning

confidence: 99%

“…The development of novel methods to simultaneously monitor multiple protein post-translational modifications (PTMs) 1 is an attractive tool for researchers. There is increasing evidence that both phosphorylation and glycosylation play important roles in cellular signaling networks during development and transformation of cells.…”

mentioning

confidence: 99%

“…Following differentiation, cells begin to migrate and associate into different brain structures. The brain structures are reorganized with the extension of axons and dendrites to communicate via synaptic terminal interactions (1,2). These molecular interactions are governed by cell surface receptors that are often post-translationally modified with both N-linked glycans and phosphate groups, and studies have suggested that extracellular glycans play vital roles in the regulation of signal transduction pathways (3).…”

mentioning

confidence: 99%

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A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

Palmisano

Parker

Engholm-Keller

et al. 2012

Molecular & Cellular Proteomics

117

105

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We describe a method that combines an optimized titanium dioxide protocol and hydrophilic interaction liquid chromatography to simultaneously enrich, identify and quantify phosphopeptides and formerly N-linked sialylated glycopeptides to monitor changes associated with cell signaling during mouse brain development. We initially applied the method to enriched membrane fractions from HeLa cells, which allowed the identification of 4468 unique phosphopeptides and 1809 formerly N-linked sialylated glycopeptides. We subsequently combined the method with isobaric tagging for relative quantification to compare changes in phosphopeptide and formerly N- The development of novel methods to simultaneously monitor multiple protein post-translational modifications (PTMs) 1 is an attractive tool for researchers. There is increasing evidence that both phosphorylation and glycosylation play important roles in cellular signaling networks during development and transformation of cells. Development of the mammalian brain is initiated during the embryonic stage and continues until adulthood. The brain originates through the proliferation of the telencephalon, the anterior part of the neural tube. Following differentiation, cells begin to migrate and associate into different brain structures. The brain structures are reorganized with the extension of axons and dendrites to communicate via synaptic terminal interactions (1, 2). These molecular interactions are governed by cell surface receptors that are often post-translationally modified with both N-linked glycans and phosphate groups, and studies have suggested that extracellular glycans play vital roles in the regulation of signal transduction pathways (3). For example, the myelin-associated glycoprotein (MAG) binds to cell surface glyco-conjugates GD1a, GT1b and Nogo receptors to form signaling complexes that inhibit axon outgrowth, whereas inhibition of Rho kinase reverses this process in a number of nerve cell types (4). There is growing evidence that both the differentiation and migration of neurons and the guidance of axons are regulated by sialic acid-containing glycoconjugates (5-7). Dietary supplementation of sialic acid leads to increases in sialic acid-containing glycoproteins in the frontal cortex and is associated with faster learning and memory in piglets (8). The nervous system contains an abundant array of sialylated molecules and it is therefore not sur-

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Section: Identification and Quantification Of Phosphopeptides And Formentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

Palmisano

Parker

Engholm-Keller

et al. 2012

Molecular & Cellular Proteomics

117

105

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“…23,24) Neurite outgrowth is regulated by a variety of signaling mechanisms, including growth factors and soluble or membrane-bound guidance cues, with coordinated regulation of the cytoskeleton within growth cones, which exhibit highly motile actin-based structures. 25) Recent studies have indicated that the Rho family of small G-proteins, Rho, Rac, and Cdc42, are key proteins in the regulation of trasnsducing signals from extracellular cues to the actin cytoskeleton.…”

Section: Virtual Cloning Of Gde2 and It's Physiological Roles Inmentioning

confidence: 99%

Mammalian Glycerophosphodiester Phosphodiesterases

Yanaka

2007

Bioscience, Biotechnology, and Biochemistry

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“…led by a growth cone, is a primary morphological event in neuronal differentiation, ultimately facilitating synaptic connections by neurons (1). Neuronal regeneration depends on the formation of neurites to repair injured or lost connections.…”

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confidence: 99%

P2Y ₂ receptor activates nerve growth factor/TrkA signaling to enhance neuronal differentiation

Arthur

Akassoglou²,

Insel³

2005

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

109

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Neurotrophins are essential for neuronal differentiation, but the onset and the intensity of neurotrophin signaling within the neuronal microenvironment are poorly understood. We tested the hypothesis that extracellular nucleotides and their cognate receptors regulate neurotrophin-mediated differentiation. We found that 5 -O-(3-thio)triphosphate (ATP␥S) activation of the G protein-coupled receptor P2Y2 in the presence of nerve growth factor leads to the colocalization and association of tyrosine receptor kinase A and P2Y2 receptors and is required for enhanced neuronal differentiation. Consistent with these effects, ATP␥S promotes phosphorylation of tyrosine receptor kinase A, early response kinase 1͞2, and p38, thereby enhancing sensitivity to nerve growth factor and accelerating neurite formation in both PC12 cells and dorsal root ganglion neurons. Genetic or small interfering RNA depletion of P2Y2 receptors abolished the ATP␥S-mediated increase in neuronal differentiation. Moreover, in vivo injection of ATP␥S into the sciatic nerve increased growth-associated protein-43 (GAP-43), a marker for axonal growth, in wild-type but not P2Y2 ؊/؊ mice. The interactions of tyrosine kinase-and P2Y 2-signaling pathways provide a paradigm for the regulation of neuronal differentiation and suggest a role for P2Y 2 as a morphogen receptor that potentiates neurotrophin signaling in neuronal development and regeneration.neurotrophin signaling ͉ P2Y2 ͉ tyrosine receptor kinase A N eurite formation, a process extending from the cell soma and led by a growth cone, is a primary morphological event in neuronal differentiation, ultimately facilitating synaptic connections by neurons (1). Neuronal regeneration depends on the formation of neurites to repair injured or lost connections. These neuronal growth events require appropriate spatial and temporal expression and action of both initiation signals and promoter molecules (2). Neurotrophins, such as nerve growth factor (NGF), are key regulators of neuronal differentiation. NGF is released by target tissues, initiates neurite generation, maintains neuronal survival, prevents apoptosis, and promotes synapse formation (3-5). NGF signaling via the tyrosine receptor kinase A (TrkA) leads to stimulation of early response kinase 1͞2 (ERK1͞2) via Ras͞Raf pathways, which is required for differentiation, as well as the activation of the survival kinase, Akt (6). The regulation of NGF͞ TrkA signaling is determined by availability of NGF, as well as TrkA activation, characterized by receptor autophosphorylation, internalization, and retrograde transport from axons to cell bodies (7). Recent evidence has shown that receptor crosstalk is an important mechanism for regulation of neurotrophin signaling (6). The NGF͞ TrkA-signaling pathway converges with pain-related ion channels to regulate NGF-mediated heat sensitivity of sensory neurons (5) and with adenosine A 2A receptors to regulate neuronal survival (8). The contributions of other signal transduction pathways integrated with NGF͞TrkA signali...

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Wiring of the brain by a range of guidance cues

Cited by 61 publications

References 139 publications

A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

Mammalian Glycerophosphodiester Phosphodiesterases

P2Y ₂ receptor activates nerve growth factor/TrkA signaling to enhance neuronal differentiation

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Wiring of the brain by a range of guidance cues

Cited by 61 publications

References 139 publications

A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

A Novel Method for the Simultaneous Enrichment, Identification, and Quantification of Phosphopeptides and Sialylated Glycopeptides Applied to a Temporal Profile of Mouse Brain Development

Mammalian Glycerophosphodiester Phosphodiesterases

P2Y 2 receptor activates nerve growth factor/TrkA signaling to enhance neuronal differentiation

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P2Y ₂ receptor activates nerve growth factor/TrkA signaling to enhance neuronal differentiation