Receptor Protein-tyrosine Phosphatase α Regulates Focal Adhesion Kinase Phosphorylation and ErbB2 Oncoprotein-mediated Mammary Epithelial Cell Motility

Boivin, Benoît; Chaudhary, Fauzia; Dickinson, Bryan C.; Haque, Aftabul; Pero, Stephanie C.; Chang, Christopher J.; Tonks, Nicholas K.

doi:10.1074/jbc.m113.527564

Cited by 17 publications

(18 citation statements)

References 78 publications

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“…The low amount and surface distribution of this non-clustered population represents very low signal in CLSM so they do not contribute to the correlation coefficients previously calculated (Fig 3B). Although they represent a low proportion of receptors in the membrane, these non-clustered ErbB2 molecules could be interacting with proteins in the FAs such as p130CAS or FAK, as described in the literature [15–21]. Our data reveal for the first time the existence of a minor population of ErbB2 within the cell membrane.…”

Section: Resultssupporting

confidence: 70%

“…Moreover, Stochastic Optical Reconstruction Microscopy (STORM) imaging showed the existence of two populations of ErbB2: a major population located in large clusters and a minor population outside these structures. The minor population is formed by low stoichiometry aggregates and would interact with FA proteins as described in the literature [15–21]. These results reveal the complexity of the ErbB2 interactome and its regulation, showing how the ECM can regulate membrane clusterization and thus the consequent availability of receptors.…”

Section: Introductionsupporting

confidence: 56%

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Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models

et al. 2017

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ErbB2 is a member of the ErbB family of tyrosine kinase receptors that plays a major role in breast cancer progression. Located at the plasma membrane, ErbB2 forms large clusters in spite of the presence of growth factors. Beta1 integrin, membrane receptor of extracellular matrix proteins, regulates adhesion, migration and invasiveness of breast cancer cells. Physical interaction between beta1 integrin and ErbB2 has been suggested although published data are contradictory. The aim of the present work was to study the interaction between ErbB2 and beta1 integrin in different scenarios of expression and activation. We determined that beta1 integrin and ErbB2 colocalization is dependent on the expression level of both receptors exclusively in adherent cells. In suspension cells, lack of focal adhesions leave integrins free to diffuse on the plasma membrane and interact with ErbB2 even at low expression levels of both receptors. In adherent cells, high expression of beta1 integrin leaves unbound receptors outside focal complexes that diffuse within the plasma membrane and interact with ErbB2 membrane domains. Superresolution imaging showed the existence of two distinct populations of ErbB2: a major population located in large clusters and a minor population outside these structures. Upon ErbB2 overexpression, receptors outside large clusters can freely diffuse at the membrane and interact with integrins. These results reveal how expression levels of beta1 integrin and ErbB2 determine their frequency of colocalization and show that extracellular matrix proteins shape membrane clusters distribution, regulating ErbB2 and beta1 integrin activity in breast cancer cells.

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Section: Resultssupporting

confidence: 70%

Section: Introductionsupporting

confidence: 56%

Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models

et al. 2017

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“…Studies have shown that SREBP-1c overexpression may lead to lipid metabolism disorder and cause lipid accumulation and fatty liver. However, there are many studies on over or low expression of SREBP-1c in rats and humans, while there have been few studies conducted in dairy cows [5,6]. Studies have shown that the fat content in the liver decreased when SREBP-1c is knocked out in ob/ob mice [7].…”

Section: Introductionmentioning

confidence: 99%

SREBP-1c Gene Silencing can Decrease Lipid Deposits in Bovine Hepatocytes Cultured <b><i>in Vitro</i></b>

Deng

Yin

et al. 2014

Cell Physiol Biochem

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Background: Fatty liver is a major metabolic disorder that occurs during early lactation in high-producing dairy cows. Sterol regulatory element-binding protein-1c (SREBP-1c) is an important transcription factor that regulates lipid synthesis by regulating the expression of lipid metabolism genes. Methods: In this study, we reduced the expression of SREBP-1c by adenovirus-mediated SREBP-1c with a low expression vector (AD-GFP-SREBP-1c) to study the effects of SREBP-1c on lipid deposits in bovine hepatocytes. The expression levels and enzyme activities of SERBP-1c and its target genes were determined by real-time PCR, western blot, and ELISA. Results: These results showed that Ad-GFP-SREBP-1c could inhibit SREBP-1c expression. The expression of the lipid synthesis enzyme acetyl-CoA carboxylase (ACC) was down-regulated. The expression levels of the lipid oxidation enzymes long-chain fatty acyl-COA synthetase (ACSL-1), carnitine palmitoyltransferase І (CPT-І), carnitine palmitoyltransferase II (CPT- II), and β-hydroxyacyl-CoA-DH (HADH) were significantly elevated. Furthermore, the expression levels of factors involved in the assembly and transport of very low-density lipoproteins (VLDLs), such as apolipoprotein B100 (ApoB), apolipoprotein E (ApoE), and microsomal triglyceride transfer protein (MTTP) were decreased comparison with the negative control and the blank control groups, but the low-density lipoprotein receptor (LDLR) was elevated. The concentrations of TG (triglyceride) and VLDL were also reduced. Conclusion: These data suggest that low SREBP-1c expression can decrease lipid synthesis, increase lipid oxidation, and decrease the TG and VLDL content in bovine hepatocytes.

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“…6 Both intra and extracellular levels of these phosphate ester-containing compounds (from now on denoted PPx) are regulated and hydrolyzed by a large number of phosphatases, releasing inorganic phosphates (Pi) as byproducts. The human genome is also encoding for hundreds of different protein phosphatases that hydrolyze phosphoric monoester modifications of proteins and that act in concert with kinases to regulate a plethora of critically important cellular processes such as metabolic activity, 7 cell motility, 8 cell survival and cell death. 9 Assays that can monitor phosphatase activity can thus be used to characterize a vast number of fundamentally important enzymatic reactions and potential drug targets and are regularly used for diagnosis of a range of diseases, and are consequently of immense importance for biomedical research, drug development, and diagnostics.…”

Section: Introductionmentioning

confidence: 99%

Generic phosphatase activity detection using zinc mediated aggregation modulation of polypeptide-modified gold nanoparticles

2014

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Receptor Protein-tyrosine Phosphatase α Regulates Focal Adhesion Kinase Phosphorylation and ErbB2 Oncoprotein-mediated Mammary Epithelial Cell Motility

Cited by 17 publications

References 78 publications

Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models

Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models

SREBP-1c Gene Silencing can Decrease Lipid Deposits in Bovine Hepatocytes Cultured <b><i>in Vitro</i></b>

Generic phosphatase activity detection using zinc mediated aggregation modulation of polypeptide-modified gold nanoparticles

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