Vimentin and the K-Ras-induced actin-binding protein control inositol-(1,4,5)-trisphosphate receptor redistribution during MDCK cell differentiation.

Dingli, Florent; Parys, Jan B.; Loew, Damarys; Saule, Simon; Méry, Laurence

doi:10.1242/jcs.108738

Cited by 12 publications

(13 citation statements)

References 45 publications

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“…As discussed above, treatment of 10 lM WFA in CHO cells induced perinuclear accumulation of vimentin filaments. Vimentin filaments in this condition are well known to be barely soluble in mild detergent such as triton X-100 [22]. We also observed a strong inverse correlation between perinuclear localization of vimentin ( Fig.…”

Section: Ser38 Residue In Vimentin Is Critical For Integrin Bindingsupporting

confidence: 70%

Vimentin filament controls integrin α5β1‐mediated cell adhesion by binding to integrin through its Ser38 residue

et al. 2016

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Regulation of integrin affinity for its ligand is essential for cell adhesion and migration. Here, we found that direct interaction of vimentin with integrin β1 can enhance binding of integrin α5β1 to its ligand, fibronectin. Conversely, blocking the interaction reduced fibronectin binding, cell migration on a fibronectin-coated surface, and neural tube closure during Xenopus embryogenesis. We also found that withaferin A (WFA), a natural compound known to inhibit vimentin function, can suppress the vimentin-integrin interaction and abolish fibronectin binding. Finally, we identified Ser38 of vimentin as a critical residue for integrin binding. Our results suggest that phosphorylation of vimentin at Ser38 may regulate the integrin-ligand interaction, thus providing a molecular basis for antivimentin therapeutic strategies.

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Section: Ser38 Residue In Vimentin Is Critical For Integrin Bindingsupporting

confidence: 70%

Vimentin filament controls integrin α5β1‐mediated cell adhesion by binding to integrin through its Ser38 residue

et al. 2016

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“…The observed proximity of IP 3 Rs to tight junctions was described before in non-transformed Madin–Darby canine kidney (MDCK) cells, where it was associated with the developed epithelial phenotype [ 30 , 39 ]. Interestingly, in our experiments this distribution was observed in the monolayers of cancer cells (PANC-1 cells) and even in relatively small clusters of these cells.…”

Section: Resultsmentioning

confidence: 56%

“…Anti-IP 3 R1 [rabbit polyclonal raised against C-terminal amino acids 2735–2749 [ 30 ] was a gift from Professor J. Parys (Catholic University of Leuven, Leuven, Belgium)]. Anti-IP 3 R1 [D53A5 (rabbit)] was from Cell Signaling Technology.…”

Section: Methodsmentioning

confidence: 99%

Epithelial–mesenchymal transition, IP3 receptors and ER–PM junctions: translocation of Ca2+ signalling complexes and regulation of migration

Okeke

Parker

Dingsdale

et al. 2016

Biochemical Journal

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Disconnection of a cell from its epithelial neighbours and the formation of a mesenchymal phenotype are associated with profound changes in the distribution of cellular components and the formation of new cellular polarity. We observed a dramatic redistribution of inositol trisphosphate receptors (IP 3 Rs) and stromal interaction molecule 1 (STIM1)-competent endoplasmic reticulum-plasma membrane junctions (ER-PM junctions) when pancreatic ductal adenocarcinoma (PDAC) cells disconnect from their neighbours and undergo individual migration. In cellular monolayers IP 3 Rs are juxtaposed with tight junctions. When individual cells migrate away from their neighbours IP 3 Rs preferentially accumulate at the leading edge where they surround focal adhesions. Uncaging of inositol trisphosphate (IP 3 ) resulted in prominent accumulation of paxillin in focal adhesions, highlighting important functional implications of the observed novel structural relationships. ER-PM junctions and STIM1 proteins also migrate to the leading edge and position closely behind the IP 3 Rs, creating a stratified distribution of Ca 2 + signalling complexes in this region. Importantly, migration of PDAC cells was strongly suppressed by selective inhibition of IP 3 Rs and store-operated Ca 2 + entry (SOCE), indicating that these mechanisms are functionally required for migration.

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“…1f-i, Supplementary Movies 2, 3) 28 . We detected no association of IP 3 Rs with intermediate filaments [29][30][31][32] (Supplementary Fig. 2, Supplementary Movie 4).…”

Section: Resultsmentioning

confidence: 88%

KRAP tethers IP3 receptors to actin and licenses them to evoke cytosolic Ca2+ signals

et al. 2021

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Regulation of IP3 receptors (IP3Rs) by IP3 and Ca2+ allows regenerative Ca2+ signals, the smallest being Ca2+ puffs, which arise from coordinated openings of a few clustered IP3Rs. Cells express thousands of mostly mobile IP3Rs, yet Ca2+ puffs occur at a few immobile IP3R clusters. By imaging cells with endogenous IP3Rs tagged with EGFP, we show that KRas-induced actin-interacting protein (KRAP) tethers IP3Rs to actin beneath the plasma membrane. Loss of KRAP abolishes Ca2+ puffs and the global increases in cytosolic Ca2+ concentration evoked by more intense stimulation. Over-expressing KRAP immobilizes additional IP3R clusters and results in more Ca2+ puffs and larger global Ca2+ signals. Endogenous KRAP determines which IP3Rs will respond: it tethers IP3R clusters to actin alongside sites where store-operated Ca2+ entry occurs, licenses IP3Rs to evoke Ca2+ puffs and global cytosolic Ca2+ signals, implicates the actin cytoskeleton in IP3R regulation and may allow local activation of Ca2+ entry.

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Vimentin and the K-Ras-induced actin-binding protein control inositol-(1,4,5)-trisphosphate receptor redistribution during MDCK cell differentiation.

Cited by 12 publications

References 45 publications

Vimentin filament controls integrin α5β1‐mediated cell adhesion by binding to integrin through its Ser38 residue

Vimentin filament controls integrin α5β1‐mediated cell adhesion by binding to integrin through its Ser38 residue

Epithelial–mesenchymal transition, IP3 receptors and ER–PM junctions: translocation of Ca2+ signalling complexes and regulation of migration

KRAP tethers IP3 receptors to actin and licenses them to evoke cytosolic Ca2+ signals

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