Annexin II binds to SHP2 and this interaction is regulated by HSP70 levels

Yoo, Jae Cheal; Hayman, Michael J.

doi:10.1016/j.bbrc.2007.03.061

Cited by 8 publications

(5 citation statements)

References 22 publications

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“…In addition, some phosphatases are preferentially localized in lipid domains [47], and thus could dephosphorylate AnxA2 at this stage. The calcium-sensitive phosphatase Src homology 2 (SH2)-containing protein tyrosine phosphatase (Shp2) is an interesting candidate because Shp2 can interact with AnxA2 in the presence of cholesterol [48,49], Shp2 is highly specific for phosphorylated AnxA2-Tyr23 [50] and Shp2 is expressed in chromaffin cells.…”

Section: Regulation Of the Anxa2-tyr23 Phosphorylation/dephosphorylat...mentioning

confidence: 99%

Phosphorylation cycling of Annexin A2 Tyr23 is critical for calcium-regulated exocytosis in neuroendocrine cells

Gabel

Delavoie

Royer

et al. 2019

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Section: Regulation Of the Anxa2-tyr23 Phosphorylation/dephosphorylat...mentioning

confidence: 99%

Phosphorylation cycling of Annexin A2 Tyr23 is critical for calcium-regulated exocytosis in neuroendocrine cells

Gabel

Delavoie

Royer

et al. 2019

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…This receptor of plasminogen activator at the membrane surface interacts with receptor tyrosine kinases like EGFR, insulin receptor (IR), insulin growth factor receptor (IGFR), and non-receptor tyrosine kinases such as Focal adhesion kinase and Src, which helps in cell signaling, angiogenesis, matrix degradation, invasion, and metastasis of cancer cells. Earlier reports have also shown that involvement of AnxA2 in internalization and sorting of EGFR in early endosomes after ligand activation [5][6][7][8].…”

Section: Introductionmentioning

confidence: 97%

Cell surface interaction of annexin A2 and galectin-3 modulates epidermal growth factor receptor signaling in Her-2 negative breast cancer cells

et al. 2015

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Overexpression and activation of tyrosine kinase receptors like EGFR and Src regulate the progression and metastasis of Her-2 negative breast cancer. Recently we have reported the role of cell membrane interaction of phospholipid-binding protein annexin A2 (AnxA2) and EGFR in regulating cellular signaling in the activation of angiogenesis, matrix degradation, invasion, and cancer metastasis. Beta-galactoside-specific animal lectin galectin-3 is an apoptosis inhibitor, and cell surface-associated extracellular galectin-3 also has a role in cell migration, cancer progression, and metastasis. Similar expression pattern and membrane co-localization of these two proteins made us to hypothesize in the current study that galectin-3 and AnxA2 interaction is critical for Her-2 negative breast cancer progression. By various experimental analyses, we confirm that glycosylated AnxA2 at the membrane surface interacts with galectin-3. N-linked glycosylation inhibitor tunicamycin treatment convincingly blocked AnxA2 membrane translocation and its association with galectin-3. To analyze whether this interaction has any functional relevance, we tried to dissociate this interaction with purified plant lectin from chickpea (Cicer arietinum agglutinin). This highly specific 30 kDa plant lectin could dissociate AnxA2 from endogenous lectin galectin-3 interaction at the cell surface. This dissociation could down-regulate Bcl-2 family proteins, cell proliferation, and migration simultaneously triggering cell apoptosis. Targeting this interaction of membrane surface glycoprotein and its animal lectin in Her-2 negative breast cancer may be of therapeutic value.

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“…The cell surface associated AnxA2 heterotetramer, is a receptor for both plasminogen and tissue type plasminogen activator (tPA) and acts as a catalytic center for the activation of plasminogen to plasmin [27,28] which helps in invasion and metastasis of cancer cells [18,27]. The membrane associated AnxA2 interacts with RTKs such as like insulin receptor (IR), insulin-like growth factor receptor (IGFR) and non-receptor tyrosine kinases such as focal adhesion kinase (FAK) and Src [29][30][31][32][33]. AnxA2 acts as a key scaffolding protein in anchoring and transportation of several proteins within plasma membrane as well as from cytosol to the plasma membrane, and contributes to cell signaling, angiogenesis and matrix degeneration [33][34][35].…”

Section: Introductionmentioning

confidence: 99%

Correction: Reciprocal Regulation of Annexin A2 and EGFR with Her-2 in Her-2 Negative and Herceptin-Resistant Breast Cancer

Shetty¹,

Thamake²,

Biswas³

et al. 2012

PLoS ONE

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Alternative survival pathways are commonly seen to be upregulated upon inhibition of receptor tyrosine kinases (RTK), including Her-2. It is established that treatment with Herceptin leads to selective overexpression and activation of epidermal growth factor receptor (EGFR) and Src which further contributes to oncogenesis in Herceptin resistant and triple negative breast cancer (TNBC) patients. Here, we show a co-regulated upregulation in the expression of Annexin A2 (AnxA2), a known substrate of Src and one of the regulators of EGFR receptor endocytosis, in Herceptin resistant and Her-2 negative breast cancer. Immunohistochemical expression analysis revealed a reciprocal regulation between Her-2 and AnxA2 in breast cancer clinical samples as well as in cell lines as confirmed by protein and RNA analysis. The siRNA and Herceptin mediated downregulation/inhibition of Her-2 in Her-2 amplified cells induced AnxA2 expression and membrane translocation. In this study we report a possible involvement of AnxA2 in maintaining constitutively activated EGFR downstream signaling intermediates and hence in cell proliferation, migration and viability. This effect was consistent in Herceptin resistant JIMT-1 cells as well as in Her-2 negative breast cancer. The siRNA mediated AnxA2 downregulation leads to increased apoptosis, decreased cell viability and migration. Our studies further indicate the role of AnxA2 in EGFR-Src membrane bound signaling complex and ligand induced activation of downstream signaling pathways. Targeting this AnxA2 dependent positive regulation of EGFR signaling cascade may be of therapeutic value in Her-2 negative breast cancer.

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Annexin II binds to SHP2 and this interaction is regulated by HSP70 levels

Cited by 8 publications

References 22 publications

Phosphorylation cycling of Annexin A2 Tyr23 is critical for calcium-regulated exocytosis in neuroendocrine cells

Phosphorylation cycling of Annexin A2 Tyr23 is critical for calcium-regulated exocytosis in neuroendocrine cells

Cell surface interaction of annexin A2 and galectin-3 modulates epidermal growth factor receptor signaling in Her-2 negative breast cancer cells

Correction: Reciprocal Regulation of Annexin A2 and EGFR with Her-2 in Her-2 Negative and Herceptin-Resistant Breast Cancer

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