The interaction of enolase-1 with caveolae-associated proteins regulates its subcellular localization

2014 ◽  
Vol 460 (2) ◽  
pp. 295-307 ◽  
Author(s):  
Dariusz Zakrzewicz ◽  
Miroslava Didiasova ◽  
Anna Zakrzewicz ◽  
Andreas C. Hocke ◽  
Florian Uhle ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Surface ◽  
Subcellular Localization ◽  
Migration And Invasion ◽  
Caveolin 1 ◽  
Annexin 2 ◽  
Associated Proteins ◽  
Surface Localization ◽  
Dependent Cell ◽  
Cell Surface Localization

We found that ENO-1 localizes to caveolae and interacts with caveolin-1 and annexin 2. The association of ENO-1 with caveolar proteins and localization within caveolae are required for ENO-1 cell surface localization and ENO-1-dependent cell migration and invasion.

scholarly journals KIF1B promotes glioma migration and invasion via cell surface localization of MT1-MMP

2015 ◽  
Vol 35 (2) ◽  
pp. 971-977 ◽  
Author(s):  
SONGYU CHEN ◽  
MINGZHI HAN ◽  
WEILIANG CHEN ◽  
YING HE ◽  
BIN HUANG ◽  
...  
Keyword(s):  
Cell Surface ◽  
Migration And Invasion ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals Tyrosine 23 Phosphorylation-Dependent Cell-Surface Localization of Annexin A2 Is Required for Invasion and Metastases of Pancreatic Cancer

PLoS ONE ◽  
2011 ◽  
Vol 6 (4) ◽  
pp. e19390 ◽  
Author(s):  
Lei Zheng ◽  
Kelly Foley ◽  
Lanqing Huang ◽  
Ashley Leubner ◽  
Guanglan Mo ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Surface ◽  
Annexin A2 ◽  
Surface Localization ◽  
Dependent Cell ◽  
Cell Surface Localization

scholarly journals EWI-2 regulates α3β1 integrin–dependent cell functions on laminin-5

2003 ◽  
Vol 163 (5) ◽  
pp. 1167-1177 ◽  
Author(s):  
Christopher S. Stipp ◽  
Tatiana V. Kolesnikova ◽  
Martin E. Hemler
Keyword(s):  
Cell Migration ◽  
Complex Formation ◽  
Cell Surface ◽  
Laminin 5 ◽  
Cell Functions ◽  
Α3β1 Integrin ◽  
Surface Localization ◽  
Dependent Cell ◽  
A Cell ◽  
Integrin Ligand

EWI-2, a cell surface immunoglobulin SF protein of unknown function, associates with tetraspanins CD9 and CD81 with high stoichiometry. Overexpression of EWI-2 in A431 epidermoid carcinoma cells did not alter cell adhesion or spreading on laminin-5, and had no effect on reaggregation of cells plated on collagen I (α2β1 integrin ligand). However, on laminin-5 (α3β1 integrin ligand), A431 cell reaggregation and motility functions were markedly impaired. Immunodepletion and reexpression experiments revealed that tetraspanins CD9 and CD81 physically link EWI-2 to α3β1 integrin, but not to other integrins. CD81 also controlled EWI-2 maturation and cell surface localization. EWI-2 overexpression not only suppressed cell migration, but also redirected CD81 to cell filopodia and enhanced α3β1–CD81 complex formation. In contrast, an EWI-2 chimeric mutant failed to suppress cell migration, redirect CD81 to filopodia, or enhance α3β1–CD81 complex formation. These results show how laterally associated EWI-2 might regulate α3β1 function in disease and development, and demonstrate how tetraspanin proteins can assemble multiple nontetraspanin proteins into functional complexes.

scholarly journals Regulation of MT1-MMP and MMP-2 by Leptin in Cardiac Fibroblasts Involves Rho/ROCK-Dependent Actin Cytoskeletal Reorganization and Leads to Enhanced Cell Migration

Endocrinology ◽  
2011 ◽  
Vol 152 (5) ◽  
pp. 2037-2047 ◽  
Author(s):  
Kristin Schram ◽  
Riya Ganguly ◽  
Eun Kyung No ◽  
Xiangping Fang ◽  
Farah S. L. Thong ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Surface ◽  
Cardiac Fibroblasts ◽  
Fiber Formation ◽  
Matrix Remodeling ◽  
Cytoskeletal Reorganization ◽  
Intact Cells ◽  
Cytoskeleton Reorganization ◽  
Surface Localization ◽  
Cell Surface Localization

Altered leptin action has been implicated in the pathophysiology of heart failure in obesity, a hallmark of which is extracellular matrix remodeling. Here, we characterize the direct influence of leptin on matrix metalloproteinase (MMP) activity in primary adult rat cardiac fibroblasts and focus on elucidating the molecular mechanisms responsible. Leptin increased expression and cell surface localization of membrane type 1 (MT1)-MMP, measured by cell surface biotinylation assay and antibody-based colorimetric detection of an exofacial epitope in intact cells. Coimmunoprecipitation analysis showed that leptin also induced the formation of a cluster of differentiation 44/MT1-MMP complex. Qualitative analysis using rhodamine-conjugated phalloidin immunofluorescence indicated that leptin stimulated actin cytoskeletal reorganization and enhanced stress fiber formation. Hence, we analyzed activation of Ras homolog gene family (Rho), member A GTPase activity and found a rapid increase in response to leptin that corresponded with increased phosphorylation of cofilin. Quantitative analysis of cytoskeleton reorganization upon separation of globular and filamentous actin by differential centrifugation confirmed the significant increase in filamentous to globular actin ratio in response to leptin, which was prevented by pharmacological inhibition of Rho (C3 transferase) or its downstream effector kinase Rho-associated coiled-coil-forming protein kinase (ROCK) (Y-27632). Inhibition of Rho or ROCK also attenuated leptin-stimulated increases in cell surface MT1-MMP content. Pro-MMP-2 is a known MT1-MMP substrate, and we observed that enhanced cell surface MT1-MMP in response to leptin resulted in enhanced extracellular activation of pro-MMP-2 measured by gelatin zymography, which was again attenuated by inhibition of Rho or ROCK. Using wound scratch assays, we observed enhanced cell migration, but not proliferation, measured by 5-bromo2′-deoxy-uridine incorporation, in response to leptin, again via a Rho-dependent signaling mechanism. Our results suggest that leptin regulates myocardial matrix remodeling by regulating the cell surface localization of MT1-MMP in adult cardiac fibroblasts via Rho/ROCK-dependent actin cytoskeleton reorganization. Subsequent pro-MMP-2 activation then contributes to stimulation of cell migration.

scholarly journals Mechanical Control of Cell Migration by the Metastasis Suppressor Tetraspanin CD82/KAI1

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1545
Author(s):  
Laura Ordas ◽  
Luca Costa ◽  
Anthony Lozano ◽  
Christopher Chevillard ◽  
Alexia Calovoulos ◽  
...  
Keyword(s):  
Cell Migration ◽  
Cell Surface ◽  
Focal Adhesion ◽  
Nuclear Translocation ◽  
Single Cells ◽  
Integral Membrane Protein ◽  
Metastasis Suppressor ◽  
Dependent Manner ◽  
Strong Inhibitor ◽  
Caveolin 1

The plasma membrane is a key actor of cell migration. For instance, its tension controls persistent cell migration and cell surface caveolae integrity. Then, caveolae constituents such as caveolin-1 can initiate a mechanotransduction loop that involves actin- and focal adhesion-dependent control of the mechanosensor YAP to finely tune cell migration. Tetraspanin CD82 (also named KAI-1) is an integral membrane protein and a metastasis suppressor. Its expression is lost in many cancers including breast cancer. It is a strong inhibitor of cell migration by a little-known mechanism. We demonstrated here that CD82 controls persistent 2D migration of EGF-induced single cells, stress fibers and focal adhesion sizes and dynamics. Mechanistically, we found that CD82 regulates membrane tension, cell surface caveolae abundance and YAP nuclear translocation in a caveolin-1-dependent manner. Altogether, our data show that CD82 controls 2D cell migration using membrane-driven mechanics involving caveolin and the YAP pathway.

Phosphorylated Caveolin-1 Regulates Rho/ROCK-Dependent Focal Adhesion Dynamics and Tumor Cell Migration and Invasion

2008 ◽  
Vol 68 (20) ◽  
pp. 8210-8220 ◽  
Author(s):  
Bharat Joshi ◽  
Scott S. Strugnell ◽  
Jacky G. Goetz ◽  
Liliana D. Kojic ◽  
Michael E. Cox ◽  
...  
Keyword(s):  
Cell Migration ◽  
Tumor Cell ◽  
Focal Adhesion ◽  
Migration And Invasion ◽  
Cell Migration And Invasion ◽  
Tumor Cell Migration ◽  
Caveolin 1

Urokinase-receptor-mediated phenotypic changes in vascular smooth muscle cells require the involvement of membrane rafts

2009 ◽  
Vol 423 (3) ◽  
pp. 343-351 ◽  
Author(s):  
Julia Kiyan ◽  
Graham Smith ◽  
Hermann Haller ◽  
Inna Dumler
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Lipid Rafts ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Caveolin 1 ◽  
Phenotypic Changes ◽  
Dependent Cell

The cholesterol-enriched membrane microdomains lipid rafts play a key role in cell activation by recruiting and excluding specific signalling components of cell-surface receptors upon receptor engagement. Our previous studies have demonstrated that the GPI (glycosylphosphatidylinositol)-linked uPAR [uPA (urokinase-type plasminogen activator) receptor], which can be found in lipid rafts and in non-raft fractions, can mediate the differentiation of VSMCs (vascular smooth muscle cells) towards a pathophysiological de-differentiated phenotype. However, the mechanism by which uPAR and its ligand uPA regulate VSMC phenotypic changes is not known. In the present study, we provide evidence that the molecular machinery of uPAR-mediated VSMC differentiation employs lipid rafts. We show that the disruption of rafts in VSMCs by membrane cholesterol depletion using MCD (methyl-β-cyclodextrin) or filipin leads to the up-regulation of uPAR and cell de-differentiation. uPAR silencing by means of interfering RNA resulted in an increased expression of contractile proteins. Consequently, disruption of lipid rafts impaired the expression of these proteins and transcriptional activity of related genes. We provide evidence that this effect was mediated by uPAR. Similar effects were observed in VSMCs isolated from Cav1−/− (caveolin-1-deficient) mice. Despite the level of uPAR being significantly higher after the disruption of the rafts, uPA/uPAR-dependent cell migration was impaired. However, caveolin-1 deficiency impaired only uPAR-dependent cell proliferation, whereas cell migration was strongly up-regulated in these cells. Our results provide evidence that rafts are required in the regulation of uPAR-mediated VSMC phenotypic modulations. These findings suggest further that, in the context of uPA/uPAR-dependent processes, caveolae-associated and non-associated rafts represent different signalling membrane domains.

scholarly journals A novel motif in the proximal C-terminus of Pannexin 1 regulates cell surface localization

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Anna L. Epp ◽  
Sarah N. Ebert ◽  
Juan C. Sanchez-Arias ◽  
Leigh E. Wicki-Stordeur ◽  
Andrew K. J. Boyce ◽  
...  
Keyword(s):  
Cell Surface ◽  
Pannexin 1 ◽  
C Terminus ◽  
Surface Localization ◽  
Cell Surface Localization

scholarly journals Cell Surface Localization of Proteolysis of Human Endothelial Angiotensin I-converting Enzyme

1995 ◽  
Vol 270 (48) ◽  
pp. 28962-28969 ◽  
Author(s):  
Véronique Beldent ◽  
Annie Michaud ◽  
Christophe Bonnefoy ◽  
Marie-Thérèse Chauvet ◽  
Pierre Corvol
Keyword(s):  
Cell Surface ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Surface Localization ◽  
Cell Surface Localization
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