Gαq-mediated plasma membrane translocation of sphingosine kinase-1 and cross-activation of S1P receptors

Braak, Michael ter; Danneberg, Kerstin; Lichte, Karin; Liphardt, Kerstin; Ktistakis, Nicholas T.; Pitson, Stuart M.; Hla, Timothy; Jakobs, Karl H.; Heringdorf, Dagmar Meyer zu

doi:10.1016/j.bbalip.2009.01.019

Cited by 32 publications

(49 citation statements)

References 62 publications

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“…Sequestration of the SK1 C-terminal sequence by partner proteins might thus conceivably unmask the membrane-interacting determinants of SK1 to facilitate membrane recruitment without phosphorylation of Ser225. This could perhaps explain a finding that G q -coupled M 3 muscarinic receptor signalling induces translocation of SK1 to the PM in a manner that is independent of Ser225 phosphorylation and changes in [Ca 2+ ] i [69]. No SK1-interacting protein partner was identified in that study, but some protein associations with the SK1 C-terminus have been established ( Figure 6).…”

Section: Sk1 (3vzb) S Aureus Dgkb (2qv7)mentioning

confidence: 91%

Sphingosine Kinases: Emerging Structure–Function Insights

Adams

Pyne

2016

Trends in Biochemical Sciences

118

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Sphingosine kinases (SK1 and SK2) catalyse the conversion of sphingosine into sphingosine 1-phosphate and control fundamental cellular processes, including cell survival, proliferation, differentiation, migration, and immune function. In this review, we highlight recent breakthroughs in the structural and functional characterisation of SK1 and these are contextualised by analysis of crystal structures for closely related prokaryotic lipid kinases. We identify a putative dimerisation interface and propose novel regulatory mechanisms governing structural plasticity induced by phosphorylation and interaction with phospholipids and proteins. Our analysis suggests that the catalytic function and regulation of the enzymes might be dependent on conformational mobility and it provides a roadmap for future interrogation of SK1 function and its role in physiology and disease.

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Section: Sk1 (3vzb) S Aureus Dgkb (2qv7)mentioning

confidence: 91%

Sphingosine Kinases: Emerging Structure–Function Insights

Adams

Pyne

2016

Trends in Biochemical Sciences

118

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“…The translocation of phospho-NIK to the outer cell membrane was unexpected but resembles changes shown upon activation of other molecules, including the catalytic subunit of (Na ϩ ϩ K ϩ )-ATPase and sphingosine kinase (SphK1) (30,31). SphK1 translocation to the plasma membrane from the cytosol involved activation of G(q)-coupled receptors, stimulation by platelet-derived growth factor, nerve growth factor, insulin-like growth factor, tumor necrosis factor-␣, IgE, lysophosphatidic acid, or methacholine, and phosphorylation of Ser 225 .…”

Section: Discussionmentioning

confidence: 99%

B-cell CLL/Lymphoma 10 (BCL10) Is Required for NF-κB Production by Both Canonical and Noncanonical Pathways and for NF-κB-inducing Kinase (NIK) Phosphorylation

Bhattacharyya

Borthakur

Tyagi

et al. 2010

Journal of Biological Chemistry

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The importance of activation of B-cell lymphoma/CLL 10 (BCL10) 2 has been recognized previously in the mucosa-associated lymphoid tissue (MALT) lymphomas, in which translocations involving MALT1 lead to constitutive activation of BCL10 and NF-B transcription (1, 2). Other reports have defined a critical role for BCL10 in the inflammatory cascade in epithelial cells, including activation by lysophosphatidic acid (3), G-protein-coupled receptor (4), and angiotensin II (5). In this report, we demonstrate that BCL10 was required for NF-B activation by both canonical and noncanonical pathways, following stimulation by the sulfated polysaccharide carrageenan (CGN) in mouse embryonic fibroblasts and in human colonic epithelial cells. Previously, we reported that CGN significantly up-regulated transcription of BCL10 in NCM460 cells (6, 7). The sulfated polysaccharide carrageenan has been widely used for decades to induce inflammation in animal and tissue culture models. In our previous work, CGN was shown to induce an inflammatory cascade in human colonic epithelial cells by two distinct mechanisms: an immune-mediated mechanism involving TLR4 (toll-like receptor 4), IRAK (IL-1␤ receptor activating kinase), BCL10, phospho-IB␣ (inhibitor of B), NF-B (nuclear factor B), and IL-8 (interleukin-8); and a reactive oxygen species (ROS)-mediated mechanism involving phospho-Hsp27, IB kinase (IKK)-␤, phospho-IB␣, BCL10, NF-B, and . Carrageenan activation of these pathways was attributable to its distinctive chemical structure, including its resemblance to the naturally occurring glycosaminoglycans, its highly sulfated galactose residues, and its unusual ␣-Gal(133)Gal bond that is a known immune epitope (10, 11). Because CGN is a commonly used food additive in the Western diet, these pathways may induce inflammation and disease in the human colon and implicate a role for BCL10 in human disease, in addition to the MALT lymphomas.To further define the BCL10-mediated activation of NF-B and the interactions between the ROS and TLR4-BCL10 pathways, the requirements for different components of the IKK signaling complex and the responses of different members of the NF-B family were investigated. The IKK signaling complex, including the catalytic components IKK␣ and IKK␤ and the regulatory component IKK␥, also known as NEMO (NF-B essential modifying factor), integrates upstream signals and leads to the phosphorylation of IB␣. Subsequently, phospho-IB␣ is ubiquitinated, and the localization signal for NF-B nuclear translocation is exposed. These events represent critical signals in the progression of the inflammatory cascade from * This work was supported in part by the Department of Veterans Affairs (to J. K. T.) and by NIDDK, National Institutes of Health Grants DK68324 and DK54016 (to P. K. D.

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“…This positive feedback loop maintains sustained activation of the SphK1-S1P axis and increased fibronectin expression leading to initiation and progression of diabetic nephropathy [44], and could also contribute to the pathogenesis of other diseases including cancer. Moreover, activation of Gq induced plasma membrane translocation of SphK1 and cross-activation of S1 PRs [45]. Hence, increased SphK1 activity and increases in S1 PR synthesis or their activations, completes this positive feedback amplification loop.…”

Section: Modified Rheostat Paradigm: Addition Of the S1p/s1pr Axismentioning

confidence: 99%