G-protein-coupled receptors and signaling networks: emerging paradigms

Marinissen, Maria Julia; Gutkind, J. Silvio

doi:10.1016/s0165-6147(00)01678-3

Cited by 920 publications

(712 citation statements)

References 72 publications

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“…Overall, we speculate that RGA cannot be a direct downstream effector of OsBRI1. Recent evidence strongly supports cross-talk between GPCRs and receptor kinases in animals [29][30][31]. Receptor kinases are also directly coupled by G proteins [32].…”

Section: Discussionmentioning

confidence: 94%

Heterotrimeric G protein α subunit is involved in rice brassinosteroid response

Wang

et al. 2006

Cell Res

111

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Heterotrimeric G proteins are known to function as messengers in numerous signal transduction pathways. The null mutation of RGA (rice heterotrimeric G protein α subunit), which encodes the α subunit of heterotrimeric G protein in rice, causes severe dwarfism and reduced responsiveness to gibberellic acid in rice. However, less is known about heterotrimeric G protein in brassinosteroid (BR) signaling, one of the well-understood phytohormone pathways. In the present study, we used root elongation inhibition assay, lamina inclination assay and coleoptile elongation analysis to demonstrated reduced sensitivity of d1 mutant plants (caused by the null mutation of RGA) to 24-epibrassinolide (24-epiBL), which belongs to brassinosteroids and plays a wide variety of roles in plant growth and development. Moreover, RGA transcript level was decreased in 24-epiBL-treated seedlings in a dose-dependent manner. Our results show that RGA is involved in rice brassinosteroid response, which may be beneficial to elucidate the molecular mechanisms of G protein signaling and provide a novel perspective to understand BR signaling in higher plants.

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Section: Discussionmentioning

confidence: 94%

Heterotrimeric G protein α subunit is involved in rice brassinosteroid response

Wang

et al. 2006

Cell Res

111

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“…MAPKs are recognized to be one of the major signaling pathways that link activation of G protein-coupled receptor to the nucleus (Bajetto et al, 2002;Marinissen and Gutkind, 2001). Our results show that in cultures of rat hippocampus CCL2 activation of CCR2 results in an increased level of phosphorylated p38 MAPK.…”

Section: Discussionmentioning

confidence: 99%

The chemokine CCL2 activates p38 mitogen-activated protein kinase pathway in cultured rat hippocampal cells

Cho

Gruol

2008

Journal of Neuroimmunology

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Emerging evidence indicates that chemokines can regulate both the physiology and biochemistry of CNS neurons and glia. In the current study, Western blot analysis showed that in rat hippocampal neuronal/glial cultures the signal transduction pathway activated by CCL2, a chemokine expressed in the normal brain and at elevated levels during neuroinflammation, involves a G-protein coupled receptor, p38 MAPK as well as its immediate upstream kinase MKK3/6, and the downstream transcription factor CREB. ERK 1/2 and the transcription factors STAT1 and STAT3 do not play a prominent role. CCL2 also altered Ca 2+ influx and synaptic network activity in the hippocampal neurons. These results suggest an important role for p38 MAPK and CREB in hippocampal actions of CCL2.

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“…Chemokines such as SDF-1 signal via heptahelical receptors. Pertussis toxinsensitive G proteins couple these receptors to phospholipase C (PLC)-␤, resulting in increases in intracellular Ca 2ϩ as well as the diacylglycerol (DAG)-dependent activation of protein kinase C (14,15). SDF-1 also activates the Fyn, Lyn, and Pyk2 tyrosine kinases, the extracellular signal-regulated kinase (ERK), and the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway (16 -18).…”

mentioning

confidence: 99%

The Rap GTPases Regulate B Cell Migration Toward the Chemokine Stromal Cell-Derived Factor-1 (CXCL12): Potential Role for Rap2 in Promoting B Cell Migration

McLeod

Lee

et al. 2002

The Journal of Immunology

110

101

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Stromal cell-derived factor-1 (SDF-1) is a potent chemoattractant for B cells and B cell progenitors. Although the binding of SDF-1 to its receptor, CXCR4, activates multiple signaling pathways, the mechanism by which SDF-1 regulates cell migration is not completely understood. In this report we show that activation of the Rap GTPases is important for B cells to migrate toward SDF-1. We found that treating B cells with SDF-1 resulted in the rapid activation of both Rap1 and Rap2. Moreover, blocking the activation of Rap1 and Rap2 via the expression of a Rap-specific GTPase-activating protein significantly reduced the ability of B cells to migrate toward SDF-1. Conversely, expressing a constitutively active form of Rap2 increased SDF-1-induced B cell migration. Thus, the Rap GTPases control cellular processes that are important for B cells to migrate toward SDF-1.

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G-protein-coupled receptors and signaling networks: emerging paradigms

Cited by 920 publications

References 72 publications

Heterotrimeric G protein α subunit is involved in rice brassinosteroid response

Heterotrimeric G protein α subunit is involved in rice brassinosteroid response

The chemokine CCL2 activates p38 mitogen-activated protein kinase pathway in cultured rat hippocampal cells

The Rap GTPases Regulate B Cell Migration Toward the Chemokine Stromal Cell-Derived Factor-1 (CXCL12): Potential Role for Rap2 in Promoting B Cell Migration

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