Differential recruitment of α2β1 and α4β1 integrins to lipid rafts in Jurkat T lymphocytes exposed to collagen type IV and fibronectin

Holleran, Brian J.; Barbar, Élie; Payet, M; Dupuis, Gilles

doi:10.1189/jlb.0902439

Cited by 21 publications

(16 citation statements)

References 64 publications

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“…We also observed that prior treatment of these cells with MbCD did not abolish calcium response to thapsigargin (Fig. 6E), thus ruling out the possibility that the observed reductions in calcium response were due to depletion of calcium reserves caused by MbCD (57). Taken together, these results demonstrate that calcium signaling is augmented in SLE T cells, at least in part, via a lipid raft-dependent mechanism.…”

Section: Enhanced Calcium Signaling In Sle T Cells Is Mediated By Lipsupporting

confidence: 62%

Alterations in Lipid Raft Composition and Dynamics Contribute to Abnormal T Cell Responses in Systemic Lupus Erythematosus

Krishnan

Nambiar

Warke

et al. 2004

The Journal of Immunology

165

147

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In response to appropriate stimulation, T lymphocytes from systemic lupus erythematosus (SLE) patients exhibit increased and faster intracellular tyrosine phosphorylation and free calcium responses. We have explored whether the composition and dynamics of lipid rafts are responsible for the abnormal T cell responses in SLE. SLE T cells generate and possess higher amounts of ganglioside-containing lipid rafts and, unlike normal T cells, SLE T cell lipid rafts include FcRγ and activated Syk kinase. IgM anti-CD3 Ab-mediated capping of TCR complexes occurs more rapidly in SLE T cells and concomitant with dramatic acceleration of actin polymerization kinetics. The significance of these findings is evident from the observation that cross-linking of lipid rafts evokes earlier and higher calcium responses in SLE T cells. Thus, we propose that alterations in the lipid raft signaling machinery represent an important mechanism that is responsible for the heightened and accelerated T cell responses in SLE.

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Section: Enhanced Calcium Signaling In Sle T Cells Is Mediated By Lipsupporting

confidence: 62%

Alterations in Lipid Raft Composition and Dynamics Contribute to Abnormal T Cell Responses in Systemic Lupus Erythematosus

Krishnan

Nambiar

Warke

et al. 2004

The Journal of Immunology

165

147

View full text Add to dashboard Cite

show abstract

“…2A, panels d-f). As previous studies have shown localization of several integrins, including ␤1, in lipid rafts of migrating cells (26,27), the putative localization of Rab1a in lipid rafts as detected by immunofluorescent staining suggests that Rab1a may affect integrin ␤1 partition in lipid rafts to regulate cell migration.…”

Section: Identification Of Rab1a As a Novel Regulator Of Cell Migration-mentioning

confidence: 99%

Regulation of Integrin β1 Recycling to Lipid Rafts by Rab1a to Promote Cell Migration

Wang

Yoo

Fan

et al. 2010

Journal of Biological Chemistry

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Rab1a is a member of the Rab family of small GTPases with a well characterized function in the regulation of vesicle trafficking from the endoplasmic reticulum to the Golgi apparatus and within Golgi compartments. The integrin family heterodimeric transmembrane proteins serve as major receptors for extracellular matrix proteins, which play essential roles in cell adhesion and migration. Although effects on intracellular trafficking of integrins or other key cargos by Rab1a could influence cell migration, the regulatory mechanisms linking Rab1a to cell migration are not well understood. Here, we report identification of Rab1a as a novel regulator of cell migration using an unbiased RNAi screen targeting GTPases. Inhibition of Rab1a reduced integrin-mediated cell adhesion and spreading on fibronectins, reduced integrin ␤1 localization to lipid rafts, and decreased recycling of integrin ␤1 to the plasma membrane. Analysis of Rab1a effector molecules showed that p115 mediated Rab1a regulation of integrin recycling and lipid raft localization in cell migration. Taken together, these results suggest a novel function for Rab1a in the regulation of cell migration through controlling integrin ␤1 recycling and localization to lipid rafts via a specific downstream effector pathway.

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“…Increasing evidence suggests that ligand-induced oligomerization causes the activation of integrins and provides the stimulus for their association with rafts (32,33). It was reasonable to expect that ligand-induced integrin oligomerization would cause their lateral association with CD157.…”

Section: And E)mentioning

confidence: 99%

The CD157-Integrin Partnership Controls Transendothelial Migration and Adhesion of Human Monocytes

Buono¹,

Parrotta²,

Morone³

et al. 2011

Journal of Biological Chemistry

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CD157, a member of the CD38 gene family, is an NAD-metabolizing ectoenzyme and a signaling molecule whose role in polarization, migration, and diapedesis of human granulocytes has been documented; however, the molecular events underpinning this role remain to be elucidated. This study focused on the role exerted by CD157 in monocyte migration across the endothelial lining and adhesion to extracellular matrix proteins. The results demonstrated that anti-CD157 antibodies block monocyte transmigration and adhesion to fibronectin and fibrinogen but that CD157 cross-linking is sufficient to overcome the block, suggesting an active signaling role for the molecule. Consistent with this is the observation that CD157 is prevalently located within the detergent-resistant membrane microdomains to which, upon clustering, it promotes the recruitment of ␤ 1 and ␤ 2 integrin, which, in turn, leads to the formation of a multimolecular complex favoring signal transduction. This functional cross-talk with integrins allows CD157 to act as a receptor despite its intrinsic structural inability to do so on its own. Intracellular signals mediated by CD157 rely on the integrin/Src/ FAK (focal adhesion kinase) pathway, resulting in increased activity of the MAPK/ERK1/2 and the PI3K/Akt downstream signaling pathways, which are crucial in the control of monocyte transendothelial migration. Collectively, these findings indicate that CD157 acts as a molecular organizer of signaling-competent membrane microdomains and that it forms part of a larger molecular machine ruled by integrins. The CD157-integrin partnership provides optimal adhesion and transmigration of human monocytes.

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Differential recruitment of α2β1 and α4β1 integrins to lipid rafts in Jurkat T lymphocytes exposed to collagen type IV and fibronectin

Cited by 21 publications

References 64 publications

Alterations in Lipid Raft Composition and Dynamics Contribute to Abnormal T Cell Responses in Systemic Lupus Erythematosus

Alterations in Lipid Raft Composition and Dynamics Contribute to Abnormal T Cell Responses in Systemic Lupus Erythematosus

Regulation of Integrin β1 Recycling to Lipid Rafts by Rab1a to Promote Cell Migration

The CD157-Integrin Partnership Controls Transendothelial Migration and Adhesion of Human Monocytes

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