The annexin 2-S100A10 complex and its association with TRPV6 is regulated by cAMP/PKA/CnA in airway and gut epithelia

Borthwick, Lee A.; Neal, Andy; Hobson, Lynsey; Gerke, Volker; Robson, Louise; Muimo, Richmond

doi:10.1016/j.ceca.2007.11.001

Cited by 41 publications

(37 citation statements)

References 59 publications

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“…Although counterintuitive at a first glance, we show that PKA (indirectly) triggers a dephosphorylation of AnxA2, thereby promoting AnxA2-S100A10 complex formation that in turn is required for efficient WPB exocytosis. As initially identified in epithelial cells, 33 this dephosphorylation is mediated by a calcineurinlike phosphatase that is activated by PKA. Thus, in line with previous observations, our results support the following order of events.…”

Section: Discussionmentioning

confidence: 97%

“…24 Thus, PKC seems to be primarily responsible for complex-destabilizing serine phosphorylation in AnxA2. In contrast, PKA through activation of a calcineurinlike phosphatase stabilizes AnxA2-S100A10 complexes by dephosphorylation of AnxA2 as shown in airway epithelial cells 33 and now in HUVECs in the course of forskolin-induced VWF secretion. The N-terminal domain of AnxA2 contains >3 putative PKC phosphorylation sites at residues Ser-11, Ser-21, and Ser-25, only one of which (Ser-11) is located in the N-terminal amphiphatic a-helix (residues 1-14) that interacts with S100A10.…”

Section: Discussionmentioning

confidence: 99%

“…Whereas PKC has been shown to catalyze Ser phosphorylation of AnxA2 in endothelial cells, thereby destabilizing the AnxA2-S100A10 complex, 24 Borthwick et al 33 have shown that a cAMP/ PKA-activated calcineurin-like phosphatase is involved in dephosphorylating AnxA2 in airway and intestinal epithelial cells, resulting in a stabilization of the complex with S100A10. Therefore, we examined whether such pathway is also triggered in forskolintreated HUVECs.…”

Section: Blood 8 August 2013 X Volume 122 Number 6 Annexin A2 Dephomentioning

confidence: 99%

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cAMP-induced secretion of endothelial von Willebrand factor is regulated by a phosphorylation/dephosphorylation switch in annexin A2

Brandherm

Disse

Zeuschner

et al. 2013

Blood

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Blood 8 August 2013 X Volume 122 Number 6 Annexin A2 Dephomentioning

confidence: 99%

See 1 more Smart Citation

cAMP-induced secretion of endothelial von Willebrand factor is regulated by a phosphorylation/dephosphorylation switch in annexin A2

Brandherm

Disse

Zeuschner

et al. 2013

Blood

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“…It is possible that the high concentration of DPP on the column was responsible for DPP displacing the other binding partners of annexin 2. Annexin 2 has been shown to form complexes with other proteins (27,28,(32)(33)(34)(35)(36). As seen in Fig.…”

Section: Discussionmentioning

confidence: 73%

“…DPP is a calcium-binding protein, and annexin 2 has been identified as a calcium and ion transport protein in kidney (27) and lung airway cells (28), both places where we have shown DPP to be expressed. For these reasons, we decided to concentrate our studies on annexin 2.…”

Section: Expression Of Phosphorylated Dpp In Baculovirus-supplementalmentioning

confidence: 99%

Dentin Phosphoprotein Binds Annexin 2 and Is Involved in Calcium Transport in Rat Kidney Ureteric Bud Cells

Alvares

Stern

Veis

2013

Journal of Biological Chemistry

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Background: Dentin phosphoprotein (DPP), responsible for tooth mineralization, is also present in nonmineralizing tissues like kidney, lung, and salivary glands. Results: DPP binds annexin 2 and 6 and plays a role in calcium influx in rat ureteric bud cells. Conclusion: DPP plays different roles in mineralizing and nonmineralizing tissues. Significance: This is the first report showing a possible function for DPP in nonmineralizing tissues.

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A2ML1and otitis media: novel variants, differential expression, and relevant pathways

Larson¹,

Magno²,

Steritz³

et al. 2019

Human Mutation

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A genetic basis for otitis media is established, however, the role of rare variants in disease etiology is largely unknown. Previously a duplication variant within A2ML1 was identified as a significant risk factor for otitis media in an indigenous Filipino population and in US children. In this report exome and Sanger sequencing was performed using DNA samples from the indigenous Filipino population, Filipino cochlear implantees, US probands, Finnish, and Pakistani families with otitis media. Sixteen novel, damaging A2ML1 variants identified in otitis media patients were rare or low-frequency in population-matched controls. In the indigenous population, both gingivitis and A2ML1 variants including the known duplication variant and the novel splice variant c.4061 + 1 G>C were independently associated with otitis media. Sequencing of salivary RNA samples from indigenous Filipinos demonstrated lower A2ML1 expression according to the carriage of A2ML1 variants. Sequencing of additional salivary RNA samples from US patients with otitis media revealed differentially expressed genes that are highly correlated with A2ML1 expression levels. In particular, RND3 is upregulated in both A2ML1 variant carriers and high-A2ML1 expressors. These findings support a role for A2ML1 in keratinocyte differentiation within the middle ear as part of otitis media pathology and the potential application of ROCK inhibition in otitis media. K E Y W O R D S A2ML1, alpha-2-macroglobulin-like-1, exome sequencing, otitis media, RNA-sequencing

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The annexin 2-S100A10 complex and its association with TRPV6 is regulated by cAMP/PKA/CnA in airway and gut epithelia

Cited by 41 publications

References 59 publications

cAMP-induced secretion of endothelial von Willebrand factor is regulated by a phosphorylation/dephosphorylation switch in annexin A2

cAMP-induced secretion of endothelial von Willebrand factor is regulated by a phosphorylation/dephosphorylation switch in annexin A2

Dentin Phosphoprotein Binds Annexin 2 and Is Involved in Calcium Transport in Rat Kidney Ureteric Bud Cells

A2ML1and otitis media: novel variants, differential expression, and relevant pathways

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