Transient Translocation of the B Cell Receptor and Src Homology 2 Domain-Containing Inositol Phosphatase to Lipid Rafts: Evidence Toward a Role in Calcium Regulation

Petrie, Ryan J.; Schnetkamp, Paul P. M.; Patel, Kamala D.; Kalia, Manjula; Deans, Julie P.

doi:10.4049/jimmunol.165.3.1220

Cited by 131 publications

(114 citation statements)

References 55 publications

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“…The lipid rafts are thought to be platforms for signaling, as Lyn kinase is concentrated within raft regions, while the phosphatase CD45 is excluded. Consistent with a role for lipid rafts in signal transduction, our recent results (16) and that of others (17,18,32) showed that both the BCR and Lyn within lipid rafts are phosphorylated in cells in which the BCR has been cross-linked. Translocation of the BCR into lipid rafts has also been shown to result in the recruitment of several components of the BCR signal cascade, including BLNK, phosphatidylinositol 3 kinase, VAV, and Btk (17,18,32).…”

Section: Discussionsupporting

confidence: 66%

“…Consistent with a role for lipid rafts in signal transduction, our recent results (16) and that of others (17,18,32) showed that both the BCR and Lyn within lipid rafts are phosphorylated in cells in which the BCR has been cross-linked. Translocation of the BCR into lipid rafts has also been shown to result in the recruitment of several components of the BCR signal cascade, including BLNK, phosphatidylinositol 3 kinase, VAV, and Btk (17,18,32). Evidence that the rafts play important physiological roles in B cell activation has been provided by the recent observations that BCR access to rafts is controlled during B cell development (19), by viral infection (20), and by the essential B cell coreceptor CD19 (Cherukuri, Sohn, and Pierce, unpublished observations).…”

Section: Discussionsupporting

confidence: 66%

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Translocation of the B Cell Antigen Receptor into Lipid Rafts Reveals a Novel Step in Signaling

Cheng

Brown

Song

et al. 2001

The Journal of Immunology

132

104

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The cross-linking of the B cell Ag receptor (BCR) leads to the initiation of a signal transduction cascade in which the earliest events involve the phosphorylation of the immunoreceptor tyrosine-based activation motifs of Igα and Igβ by the Src family kinase Lyn and association of the BCR with the actin cytoskeleton. However, the mechanism by which BCR cross-linking initiates the cascade remains obscure. In this study, using various A20-transfected cell lines, biochemical and genetic evidence is provided that BCR cross-linking leads to the translocation of the BCR into cholesterol- and sphingolipid-rich lipid rafts in a process that is independent of the initiation of BCR signaling and does not require the actin cytoskeleton. Translocation of the BCR into lipid rafts did not require the Igα/Igβ signaling complex, was not dependent on engagement of the FcR, and was not blocked by the Src family kinase inhibitor PP2 or the actin-depolymerizing agents cytochalasin D or latrunculin. Thus, cross-linking or oligomerization of the BCR induces the BCR translocation into lipid rafts, defining an event in B cell activation that precedes receptor phosphorylation and association with the actin cytoskeleton.

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Section: Discussionsupporting

confidence: 66%

Section: Discussionsupporting

confidence: 66%

Translocation of the B Cell Antigen Receptor into Lipid Rafts Reveals a Novel Step in Signaling

Cheng

Brown

Song

et al. 2001

The Journal of Immunology

132

104

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“…The insoluble fraction may function as a domain within the cell where signaling factors such as TRAF6 and Src are active or activated. This is supported by the fact that Lyn and Lck also display altered localization into raft domain during BCR-or TCR-CD28-mediated signaling, respectively (Janes et al, 1999;Petrie et al, 2000). Additionally, as previously mentioned, TRAF6 translocation to nonionic detergentinsoluble fraction is necessary for exerting its biological role during TRANCE signaling (Ha et al, 2003).…”

Section: Discussionsupporting

confidence: 48%

“…Phosphorylation of Tyr416 in the activation loop of SH1 kinase domain elevates the enzyme activity whereas phosphorylation of Tyr527 in the C-terminal tail by Csk reduces the enzyme activity (Fujimoto et al, 2000). Activated Src family kinases have been preferentially found in raft domain (Kramer et al, 1999;Petrie et al, 2000;Dykstra et al, 2001), which is enriched in sphingolipids and cholesterol and displays a resistance to a nonionic detergent such as TritonX-100 (Brown and London, 2000). Interestingly, it has been reported that TRAF6 enhances Src STP-A11, an oncoprotein of Herpesvirus saimiri augments both NF-κB and AP-1 transcription activity through TRAF6 activity upon TRANCE signaling in dendritic cells and osteoclast cells (Wong et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

STP-A11, an oncoprotein of Herpesvirus saimiri augments both NF-κB and AP-1 transcription activity through TRAF6

Jeong

Cho²,

An³

et al. 2007

Exp Mol Med

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Herpesvirus saimiri (HVS), a member of the γ-herpesvirus family, encodes an oncoprotein called Saimiri Transforming Protein (STP) which is required for lymphoma induction in non-human primates. However, a detailed mechanism of STP-A11-induced oncogenesis has not been revealed yet. We first report that STP-A11 oncoprotein interacts with TNFreceptor-associated factor (TRAF) 6 in vivo and in vitro. Mutagenesis analysis of the TRAF6-binding motif 10 PQENDE 15 in STP-A11 reveals that Glu (E) 12 residue is critical for binding to TRAF6 and NF-κB activation. Interestingly, co-expression of E12A mutant, lack of TRAF6 binding, with cellular Src (Src) results in decreased transcriptional activity of Stat3 and AP-1, a novel target of STP-A11 compared to that of wild type. Furthermore, the presence of STP-A11 enhances the association of TRAF6 with Src and induces the translocation of both TRAF6 and Src to a nonionic detergent-insoluble fraction. Taken together, these studies suggest that STP-A11 oncoprotein up-regulates both NF-κB and AP-1 transcription activity through TRAF6, which would ultimately contribute cellular transformation.

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“…5, a and b) (43,45,46). It is generally accepted, despite a lack of mechanistic description, that integrity of the lipid raft is essential for many functions downstream of integrin signaling (33), including calcium mobilization (47) and thrombosis (35). Our results support this notion by raising a mechanistic example showing that lipid rafts, by "corralling" NHE1 and NCX1 to the vicinity, are able to facilitate functional coupling between the two "interacting" molecules and trigger important signaling downstream of integrin.…”

Section: And 5)mentioning

confidence: 99%

Membrane Targeting and Coupling of NHE1-IntegrinαIIbβ3-NCX1 by Lipid Rafts following Integrin-Ligand Interactions Trigger Ca2+ Oscillations

Yi¹,

Ho²,

Chen³

et al. 2009

Journal of Biological Chemistry

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The cyclic calcium release and uptake during calcium oscillation are thought to result from calcium-induced calcium release (CICR); however, it is unclear, especially in nonexcitable cells, how the initial calcium mobilization that triggers CICR occurs. We report here a novel mechanism, other than conventional calcium channels or the phopholipase C-inositol trisphosphate system, for initiating calcium oscillation downstream of integrin signaling. Upon integrin ␣ IIb ␤ 3 binding to fibrinogen ligand or the disintegrin rhodostomin, sodium-proton exchanger NHE1 and sodiumcalcium exchanger NCX1 are actively transported to the plasma membrane, and they become physically coupled to integrin ␣ IIb ␤ 3 . Lipid raft-dependent mechanisms modulate the membrane targeting and formation of the NHE1-integrin ␣ IIb ␤ 3 -NCX1 protein complex. NHE1 and NCX1 within such protein complex are functionally coupled, such that a local increase of sodium concentration caused by NHE1 can drive NCX1 to generate sodium efflux in exchange for calcium influx. The resulting calcium increase inside the cell can then trigger CICR as a prelude to calcium oscillation downstream of integrin ␣ IIb ␤ 3 signaling. Fluorescence resonance energy transfer based on fluorescence lifetime measurements is employed here to monitor the intermolecular interactions among NHE1-integrin ␣ IIb ␤ 3 -NCX1, which could not be properly detected using conventional biochemical assays.In many excitable or nonexcitable cells, the concentration of free intracellular calcium oscillates with a period ranging from a few seconds to a few minutes. Such calcium oscillations are involved in a wide variety of cellular functions (1, 2). It is generally believed that, except for minor variations, the cyclic increase and decrease of calcium results from an autocatalytic release of calcium in a process called calcium-induced calcium release (CICR), 2 followed by a slow negative feedback that terminates calcium release. The cytoplasmic free calcium is then taken up into the organelles to reset the cycle. Despite a general agreement on how calcium oscillation proceeds once the system has been turned on, various different mechanisms have been proposed to explain how the initial calcium mobilization is generated that triggers CICR.As a general rule, calcium entry through voltage-gated channels in electrically excitable cells (3) or through agonist-receptor interactions in nonexcitable cells, such as epithelial cells, hepatocytes, or oocytes (4), is thought to initiate the CICR process (1, 2). Typically, in nonexcitable cells, the binding of an agonist, such as a hormone, a growth factor, or an extracellular matrix, to the corresponding cell surface receptor initiates a series of reactions that end in the activation of phopholipase C (PLC) and the production of the secondary messenger inositol trisphosphate (IP 3 ) (1, 2, 4). IP 3 is thought to induce calcium release from the internal endoplasmic reticulum or mitochondria store, and governs the CICR mechanisms that modulate calcium oscillat...

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Transient Translocation of the B Cell Receptor and Src Homology 2 Domain-Containing Inositol Phosphatase to Lipid Rafts: Evidence Toward a Role in Calcium Regulation

Cited by 131 publications

References 55 publications

Translocation of the B Cell Antigen Receptor into Lipid Rafts Reveals a Novel Step in Signaling

Translocation of the B Cell Antigen Receptor into Lipid Rafts Reveals a Novel Step in Signaling

STP-A11, an oncoprotein of Herpesvirus saimiri augments both NF-κB and AP-1 transcription activity through TRAF6

Membrane Targeting and Coupling of NHE1-IntegrinαIIbβ3-NCX1 by Lipid Rafts following Integrin-Ligand Interactions Trigger Ca2+ Oscillations

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