| 2003 |
S100A10 (p11) was identified as the first auxiliary protein of the epithelial Ca2+ channels TRPV5 and TRPV6 via yeast two-hybrid and GST pull-down. S100A10 binds the conserved C-terminal VATTV motif of TRPV5/TRPV6 (first threonine critical); S100A10 forms a heterotetrameric complex with annexin A2 that routes TRPV5 and TRPV6 to the plasma membrane. Annexin A2-specific siRNA knockdown inhibited TRPV5/TRPV6-mediated currents in HEK293 cells. |
Yeast two-hybrid, GST pull-down, co-immunoprecipitation, siRNA knockdown, electrophysiology, site-directed mutagenesis |
The EMBO journal |
High |
12660155
|
| 1997 |
S100A10 (calpactin light chain) was identified as a component of the cornified envelope (CE) of cultured human epidermal keratinocytes, cross-linked via epsilon-(gamma-glutamyl)lysine bonds; its reactive sites were mapped by sequential proteolytic digestion to amino- and carboxyl-terminal regions. |
Proteolytic cleavage of purified CE fragments followed by peptide sequencing (CNBr digestion, trypsin, proteinase K) |
The Journal of biological chemistry |
Medium |
9115270
|
| 2003 |
In Madin-Darby canine kidney (MDCK) cells, S100A10 mediates the interaction between annexin A2 and the C-terminal regulatory domain of AHNAK at the plasma membrane. The annexin A2/S100A10 complex is required for AHNAK plasma membrane association; siRNA knockdown of both proteins prevented AHNAK plasma membrane localization and impaired cortical actin cytoskeleton reorganization needed to support cell height. |
Co-immunoprecipitation, siRNA knockdown, actin cytoskeleton imaging, cell fractionation |
The Journal of cell biology |
High |
14699089
|
| 2003 |
The annexin A2/S100A10 heterotetramer (AIIt) bound t-PA (Kd=0.68 µM), plasminogen (Kd=0.11 µM), and plasmin (Kd=75 nM) when immobilized on a phospholipid bilayer; the carboxyl-terminal lysines of S100A10 form the t-PA and plasminogen binding sites, while annexin A2 and S100A10 contain distinct binding sites for plasmin. |
Surface plasmon resonance on phospholipid-immobilized protein, carboxyl-terminal lysine removal |
The Journal of biological chemistry |
High |
12730231
|
| 2003 |
Downregulation of annexin A2 and S100A10 by siRNA perturbed the distribution of transferrin receptor- and rab11-positive recycling endosomes (producing extensively bent tubules and increased clathrin-positive buds) but did not significantly affect transferrin uptake/recycling kinetics. Rescue by reexpression of the N-terminal annexin A2 domain or S100A10 confirmed both subunits are required for proper positioning of recycling endosomes. |
RNAi knockdown, immunofluorescence, whole-mount immunoelectron microscopy, transferrin uptake assay, rescue by reexpression |
Molecular biology of the cell |
High |
13679511
|
| 2003 |
siRNA-mediated stable knockdown of S100A10 in colorectal CCL-222 cancer cells caused 45% loss in plasminogen binding, 65% loss in cellular plasmin generation, and complete loss of plasminogen-dependent invasiveness. S100A10 was shown to associate with the plasma membrane and co-localize with uPAR independently of annexin A2. |
Stable RNAi knockdown (pSUPER vector), plasminogen binding assay, plasmin generation assay, invasion assay |
The Journal of biological chemistry |
High |
14570893
|
| 2005 |
S100A10, S100A7, and S100A11 are substrates for both type I and type II transglutaminases, which catalyze epsilon-(gamma-glutamyl)lysine crosslinks; the reactive residues are located at the solvent-exposed amino- and carboxyl-terminal ends of S100A10. |
In vitro transglutaminase enzymatic assay |
Biochemistry |
Medium |
11258932
|
| 2008 |
In endothelial cells, unpartnered S100A10 (p11) is polyubiquitinated and degraded via a proteasome-dependent mechanism. Annexin A2 (A2) stabilizes intracellular S100A10 through direct binding, masking an autonomous S100A10 polyubiquitination signal; this interaction requires both the p11-binding N-terminal domain of A2 and the C-terminal domain of p11. p11 is also required for Src kinase-mediated tyrosine phosphorylation of A2, which signals translocation of both proteins to the cell surface. |
In vitro and in vivo co-immunoprecipitation, ubiquitination assay, proteasome inhibition, endothelial cell fractionation, A2 knockout cell/mouse model |
The Journal of biological chemistry |
High |
18434302
|
| 2004 |
The annexin II-S100A10 complex is required for formation of E-cadherin-based adherens junctions in MDCK cells. Depletion of plasma membrane cholesterol (abolishing complex localization) or knockdown of annexin II by RNAi inhibited re-concentration of E-cadherin at nectin-based cell-cell contact sites during Ca2+ switch experiments. |
RNAi knockdown, cholesterol depletion, Ca2+ switch assay, immunofluorescence |
The Journal of biological chemistry |
Medium |
15574423
|
| 2005 |
The annexin A2/S100A10 heterotetramer (A2t) induces lateral segregation of phosphatidylserine (POPS)-enriched membrane domains in artificial phospholipid bilayers, forming micrometer-sized protein domains associated with POPS depletion in neighboring membrane areas. |
Scanning force microscopy, fluorescence microscopy on artificial lipid bilayers |
Biochemistry |
Medium |
16285733
|
| 2001 |
Annexin A2 is the plasma membrane-targeting subunit of the annexin A2/S100A10 complex: monomeric annexin A2 is targeted to the plasma membrane, while non-complexed S100A10 distributes to the general cytosol; co-expression and complex formation recruits S100A10 to the plasma membrane. |
Live cell imaging with YFP/CFP fusion proteins in HepG2 cells |
FEBS letters |
Medium |
11445072
|
| 2006 |
Annexin A2 is required for strong binding of S100A10 to the C-terminal domain of AHNAK in a yeast triple-hybrid experiment and in vitro binding assay; the Annexin A2 N-terminal tail (involved in S100A10/Annexin A2 tetramerization) mediates this effect. The minimal A2t binding motif in AHNAK was mapped to a 20-amino-acid peptide (A2tBP1), and a second lower-affinity motif (A2tBP2) was identified in the AHNAK N-terminal domain. |
Yeast triple-hybrid, in vitro binding assay, co-immunoprecipitation, live cell imaging with EGFP fusion |
The Journal of biological chemistry |
High |
16984913
|
| 2005 |
The annexin A2/S100A10 heterotetramer (AIIt) directly reduces the disulfide bond of plasmin (Cys462-Cys541) during plasmin autoproteolysis; AIIt thiols are oxidized during plasmin disulfide reduction. Thioredoxin reductase uses NADPH to recycle oxidized thioredoxin, which in turn reduces oxidized AIIt, completing an electron transfer chain from NADPH to AIIt. AIIt is identified as a substrate of the thioredoxin system. |
In vitro thiol oxidation assay (MBP-biocytin labeling), NADPH/thioredoxin reductase reconstitution, cell-based plasminogen treatment assay |
The Journal of biological chemistry |
High |
15849182
|
| 2007 |
S100A10 (p11) is dispensable for annexin A2 association to early endosomes and for early-to-late endosome transport. Biochemical fractionation showed p11 was not present on purified early endosomes, and p11 siRNA knockdown did not affect annexin A2 targeting to early endosomes or endosomal transport beyond early endosomes (in contrast to annexin A2 knockdown). |
siRNA knockdown, early endosome purification, immunofluorescence, endosomal transport assay (in vitro liposome binding) |
PloS one |
High |
17971878
|
| 2007 |
A cAMP/PKA/calcineurin (CnA)-dependent mechanism regulates annexin 2-S100A10 complex formation and its interaction with CFTR chloride channel. Forskolin increased annexin 2-S100A10 co-immunoprecipitation with cell surface CFTR; this was attenuated by PKA or CnA inhibitors. An acetylated peptide covering the S100A10-binding site on annexin 2 (Ac1-14) disrupted the complex and inhibited cAMP/PKA-dependent CFTR-mediated and outwardly rectifying chloride channel currents. |
Co-immunoprecipitation, electrophysiology (patch clamp), peptide competition, PKA/CnA inhibitors, short-circuit current across intestinal biopsy |
Molecular biology of the cell |
High |
17581860
|
| 2007 |
The annexin II-S100A10 complex forms a ternary complex with tryptophanyl-tRNA synthetase (TrpRS) and regulates trafficking of TrpRS for exocytosis from endothelial cells; both annexin II and S100A10 are required for TrpRS secretion. |
Co-immunoprecipitation, pulldown, trafficking/secretion assay |
The Journal of biological chemistry |
Medium |
17999956
|
| 2008 |
In CFBE41o- cells homozygous for F508del-CFTR (ΔF508), cAMP/PKA fails to induce annexin 2-S100A10/CFTR complex formation, due to defective PKA-dependent serine phosphorylation of calcineurin A (CnA), defective CnA-annexin 2 complex formation, and defective CnA-dependent dephosphorylation of annexin 2. |
Co-immunoprecipitation, western blotting, immunohistochemistry, CF mouse model |
Cellular signalling |
Medium |
18346874
|
| 2010 |
S100A10 acts as a cell surface plasminogen receptor on macrophages; S100A10-deficient mice showed up to 53% reduction in macrophage migration into the peritoneal cavity in response to thioglycollate, 8-fold fewer macrophages in Matrigel plugs in vivo, 50% reduction in plasmin-dependent invasion, and 45% reduction in plasmin generation in vitro. Loss of S100A10 reduced pro-MMP-9 activation. |
S100A10 knockout mouse model, Matrigel invasion assay, plasmin generation assay, peritoneal lavage, in vivo Matrigel plug assay, MMP-9 activation assay |
Blood |
High |
20424186
|
| 2010 |
S100A10 co-localizes and directly interacts with VAMP2 (synaptobrevin 2) at the plasma membrane of resting adrenergic chromaffin cells; S100A10 is present in VAMP2 microdomains. Stimulation induces annexin A2 translocation to the plasma membrane where it interacts with S100A10 to form a tetramer. Tetanus toxin cleavage of VAMP2 solubilizes S100A10 from the plasma membrane and inhibits annexin A2 translocation, indicating S100A10 plasma membrane anchoring depends on VAMP2. |
Cross-linking, co-immunoprecipitation, immunogold labeling with spatial point pattern analysis, tetanus toxin treatment, confocal microscopy |
Traffic (Copenhagen, Denmark) |
High |
20374557
|
| 2011 |
S100A10-deficient mice display increased fibrin deposition in vasculature and reduced clearance of batroxobin-induced vascular thrombi; S100A10-null endothelial cells showed 40% reduction in plasminogen binding and plasmin generation in vitro, and impaired neovascularization of Matrigel plugs in vivo, establishing S100A10 as a regulator of fibrinolysis and angiogenesis. |
S100A10 knockout mouse model, fibrin staining, thrombolysis assay, plasminogen binding, plasmin generation, Matrigel plug assay |
Blood |
High |
21768297
|
| 2011 |
DLC1 tumor suppressor directly binds S100A10 via central sequences in DLC1 and the C-terminus of S100A10—the same C-terminal region used by annexin A2. DLC1 competes with annexin A2 for S100A10 binding, displacing S100A10 from annexin A2 and making it accessible to ubiquitin-dependent proteasomal degradation, thereby decreasing S100A10 levels, attenuating plasminogen activation, and inhibiting cancer cell migration, invasion, and anchorage-independent growth. |
Co-immunoprecipitation, competition binding assay, quantitative invasion/migration assays, ubiquitination assay, siRNA knockdown |
Cancer research |
High |
21372205
|
| 2011 |
PML-RARα oncoprotein increases cell surface S100A10 in APL cells; treatment with all-trans retinoic acid (ATRA) rapidly downregulates S100A10, concomitant with loss of fibrinolytic activity. S100A10 siRNA depletion blocked enhanced fibrinolytic activity of PML-RARα-expressing cells. |
Western blot, ATRA treatment, RNAi knockdown, plasmin generation assay, flow cytometry |
Blood |
Medium |
21310922
|
| 2011 |
The S100A10-annexin A2 ternary complex with AHNAK has an asymmetric arrangement: a single AHNAK peptide binds the A2t dimer at a site comprising residues from helix IV of S100A10 and the C-terminal portion of the annexin A2 N-terminal peptide, as determined by NMR and biophysical analysis. This binding surface is distinct from previously identified S100 target protein interfaces. |
NMR spectroscopy, multiple biophysical methods (SPR, ITC), peptide binding assays |
The Journal of biological chemistry |
High |
21949189
|
| 2011 |
Genetic deletion of S100A10 in mice dramatically reduced growth of Lewis lung carcinomas and T241 fibrosarcomas, corresponding to decreased macrophage density at tumor sites. Intraperitoneal injection of wild-type (but not S100A10-deficient) macrophages rescued tumor growth in S100A10-null mice; direct intratumoral injection of either genotype rescued growth, demonstrating S100A10 is required specifically for macrophage migration to tumors. |
S100A10 knockout mouse model, syngeneic tumor implantation, macrophage reconstitution (IP and intratumoral injection), macrophage depletion |
Cancer research |
High |
22042827
|
| 2012 |
The S100A10 subunit of the annexin A2 heterotetramer (A2t) interacts with the HPV16 L2 minor capsid protein at aa 108-120 (as shown by EPR), and this interaction promotes HPV16 particle internalization; mutation of this L2 region reduces A2t binding and HPV16 pseudovirus infection. ShRNA downregulation of A2t decreases capsid internalization and infection. |
Co-immunoprecipitation, electron paramagnetic resonance (EPR), shRNA knockdown, L2 mutagenesis, infection assay |
PloS one |
High |
22927980
|
| 2012 |
Crystal structure of the AHNAK C-terminal 20-aa peptide bound to the AnxA2-S100A10 heterotetramer (1:2:2 asymmetric complex) at 2.5 Å resolution confirmed asymmetric binding mode; AHNAK binding is governed by hydrophobic interactions with pockets on S100A10 and hydrogen bonds involving AHNAK backbone atoms, explaining high affinity and broad consensus sequence for S100A10 binding. |
X-ray crystallography (2.5 Å resolution) |
Acta crystallographica. Section D, Biological crystallography |
High |
23275167
|
| 2012 |
N-terminal acetylation of annexin A2 (removal of Met1, acetylation of Ser2) is required for S100A10 binding. Acetylated but not non-acetylated peptides covering the N-terminal annexin A2 sequence competitively inhibit complex formation, and N-terminally acetylated annexin A2 forms heterotetramer with S100A10 with affinity comparable to porcine tissue-derived AnxA2. |
Competitive peptide inhibition assay, mass spectrometry (N-terminal modification analysis), isothermal titration calorimetry/binding affinity assay |
Biological chemistry |
High |
23091277
|
| 2012 |
S100A10 is required for actin stress fiber organization and cell spreading. Depletion of S100A10 impaired stress fiber formation and delayed cell spreading; Rac1 activation during spreading was suppressed by S100A10 knockdown, and expression of constitutively active Rac1 rescued spreading in S100A10-depleted cells. |
siRNA knockdown, actin staining, cell spreading assay, Rac1 activation assay, constitutively active Rac1 rescue |
Molecular and cellular biochemistry |
Medium |
23129259
|
| 2013 |
HPV16 exposure to keratinocytes induces EGFR-dependent Src kinase activation that phosphorylates and promotes extracellular translocation of annexin A2. HPV16 particles interact with AnxA2-S100A10 heterotetramer at the cell surface in a Ca2+-dependent manner; anti-AnxA2 antibody prevents HPV16 internalization, while anti-S100A10 antibody blocks infection at a late endosomal/lysosomal site, suggesting separate roles for AnxA2 (entry) and S100A10 (intracellular trafficking). |
Co-immunoprecipitation, antibody blockade, siRNA knockdown, confocal microscopy, infection assay |
Journal of virology |
High |
23637395
|
| 2016 |
S100A10 regulates ULK1 localization to autophagosome formation sites at ER-mitochondria contact sites during IFN-γ-triggered autophagy. S100A10 interacts with ULK1 after IFN-γ stimulation; S100A10 knockdown prevents ULK1 localization to autophagosome formation sites and reduces autophagosome formation. ANXA2 acts upstream: ANXA2 knockdown reduces S100A10 expression, but S100A10 overexpression in ANXA2-knockdown cells restores autophagosome formation. |
Co-immunoprecipitation, siRNA knockdown, overexpression rescue, immunofluorescence, autophagy assay (autophagosome counting) |
Journal of molecular biology |
Medium |
27871932
|
| 2016 |
Oncogenic KRAS increases S100A10 gene expression via the RalGDS pathway, leading to increased cell surface S100A10 protein and elevated cellular plasmin generation; depletion of S100A10 from RAS-transformed cells reduced both plasmin generation and invasiveness. |
Oncogenic RAS expression, RAS effector-loop mutants, S100A10 gene expression analysis, siRNA knockdown, plasmin generation assay, invasion assay |
Oncotarget |
Medium |
27351226
|
| 2017 |
S100A10 binds the Munc13-4 secretory protein; the AnxA2-S100A10 complex recruits Munc13-4 to Weibel-Palade body (WPB) fusion sites at the plasma membrane, promoting histamine-evoked WPB exocytosis and von Willebrand factor release. |
Co-immunoprecipitation, siRNA knockdown, total internal reflection fluorescence (TIRF) microscopy, VWF release assay |
Molecular biology of the cell |
Medium |
28450451
|
| 2017 |
The kringle-2 domain of tPA (not the finger domain as in fibrin-stimulated plasmin generation) is critical for S100A10-dependent plasmin generation; the kringle-1 domain of plasminogen is also critical for S100A10-dependent (but not fibrin-dependent) plasminogen activation. Internal lysine residues of S100A10 contribute to plasmin-generating activity even after deletion/substitution of carboxyl-terminal lysine. |
Domain-switched/deleted tPA variants, truncated plasminogen variants, S100A10 site-directed mutagenesis, in vitro plasmin generation assay |
Thrombosis and haemostasis |
High |
28382372
|
| 2017 |
PLA2R (phospholipase A2 receptor) from podocytes binds specifically to the S100A10 component of the annexin A2-S100A10 (A2t) complex with high affinity; binding increases in acidic pH and occurs within the PLA2R NC3 fragment. Ca2+ promotes PLA2R-A2t complex association with phospholipid membranes in vitro. All three proteins co-localize in podocyte plasma membrane and extracellular vesicles. |
Proteomics pull-down, surface plasmon resonance, domain mapping, in vitro lipid membrane binding, co-localization by confocal microscopy |
Scientific reports |
High |
28761153
|
| 2018 |
S100A10 is succinylated at lysine residue K47 by CPT1A acting as a lysine succinyltransferase; SIRT5 acts as the desuccinylase. K47 succinylation stabilizes S100A10 by suppressing ubiquitylation and proteasomal degradation. Expression of a succinylation-mimetic K47E mutant increased gastric cancer cell invasion and migration. |
Mass spectrometry (succinylation identification), co-immunoprecipitation (CPT1A-S100A10), overexpression of K47E mutant, ubiquitination assay, invasion/migration assay, SIRT5 manipulation |
Journal of cellular and molecular medicine |
High |
30394687
|
| 2018 |
Annexin A2 heterotetramer (A2t) including S100A10 is required for HPV intracellular trafficking from early to multivesicular endosomes, capsid uncoating, and protection from lysosomal degradation. Without A2t, viral progression from early endosomes is inhibited, uncoating dramatically reduced, and lysosomal degradation accelerated. AnxA2 forms a complex with CD63, a mediator of HPV trafficking. |
S100A10 shRNA knockdown, electron microscopy, co-immunoprecipitation, infection assay |
Scientific reports |
Medium |
30076379
|
| 2018 |
ATRA promotes proteasomal degradation of S100A10 (p11) in an ubiquitin-independent manner in APL cells (NB4); proteasomal inhibitor lactacystin reversed ATRA-dependent p11 loss but did not cause accumulation of ubiquitylated p11. ATRA also reduces p11 transcript and protein independently of PML-RARα (in MCF-7 cells). Overexpression of annexin A2 upregulates p11 protein but not mRNA post-translationally. Forced expression of ubiquitin and p11 identified K57 as the ubiquitylation site of p11. |
Proteasome inhibition (lactacystin), siRNA, ubiquitin overexpression with site-directed mutagenesis (K57), western blot, RT-PCR |
Cell death & disease |
High |
30206209
|
| 2019 |
GAS6/AXL signaling activates S100A10 expression through SRC to promote plasmin production, endothelial cell invasion, and angiogenesis in ccRCC. Genetic and therapeutic inhibition of AXL signaling reduced tumor vessel density, S100A10 expression, and ccRCC growth in xenograft models. |
Genetic AXL inhibition, small molecule AXL inhibitor (cabozantinib), sAXL decoy receptor, tumor xenograft, angiogenesis assays, western blot |
Cancer research |
Medium |
31585940
|
| 2019 |
S100A10 is constitutively expressed in macrophages but is significantly downregulated upon TLR activation. S100A10-deficient macrophages are hyperresponsive to TLR stimulation; S100A10-deficient mice are more sensitive to endotoxin-induced lethal shock and E. coli-induced abdominal sepsis. Mechanistically, S100A10 interferes with recruitment and activation of receptor-proximal TLR signaling components to inhibit downstream TLR signaling. |
S100A10 knockout mouse model, TLR stimulation assays, cytokine measurement, endotoxin shock model, sepsis model, signaling component analysis |
Cellular & molecular immunology |
Medium |
31467414
|
| 2020 |
Paclitaxel-induced HIF-1-dependent S100A10 expression leads to complex formation of S100A10 with ANXA2, SPT6, and KDM6A; this complex is recruited to OCT4 binding sites where KDM6A erases H3K27me3 marks to facilitate transcription of pluripotency genes (NANOG, SOX2, KLF4), specifying breast cancer stem cells. S100A10 silencing blocks chemotherapy-induced BCSC enrichment and impairs tumor initiation. |
Co-immunoprecipitation, ChIP, siRNA/shRNA knockdown, HIF-1 manipulation, tumor initiation assay, chromatin mark analysis |
The Journal of clinical investigation |
High |
32427586
|
| 2020 |
S100A10 promotes aerobic glycolysis and malignant growth in gastric cancer by activating mTOR signaling through interaction with ANXA2, via the Src/ANXA2/AKT/mTOR signaling pathway. |
Co-immunoprecipitation, siRNA knockdown, glycolysis assays (glucose consumption, lactate, OCR, ECAR), western blot (signaling), xenograft model |
Frontiers in cell and developmental biology |
Medium |
33324631
|
| 2021 |
SUMOylation of S100A10 promotes its nuclear localization in polyploid giant cancer cells (PGCCs) and daughter cells; in contrast, control cells show predominantly ubiquitinated S100A10 (cytoplasmic). Nuclear S100A10 regulates expression of ARHGEF18, PTPRN2, and DEFA3 (involved in actin dynamics and cytoskeleton remodeling), as shown by ChIP-Seq. Inhibition of SUMO1 reduces nuclear S100A10 and decreases proliferation/migration of PGCCs. |
Co-immunoprecipitation, MG132 and ginkgolic acid treatment, western blot, ChIP-Seq, SUMO1 inhibition |
Frontiers in cell and developmental biology |
Medium |
34336846
|
| 2023 |
ANXA2 and S100A10 accumulate in apically extruded, RasV12-transformed epithelial cells; ANXA2 acts upstream of S100A10 accumulation. ANXA2 knockdown promotes apoptosis of apically extruded transformed cells via ROS-mediated p38MAPK activation; the p38MAPK inhibitor and ROS scavenger Trolox rescue the multilayered structure phenotype, defining an ANXA2/S100A10 → ROS/p38MAPK pathway that prevents anoikis of transformed cells. |
siRNA/shRNA knockdown, in vitro and in vivo (murine tissue) imaging, ROS measurement, p38MAPK inhibition, Trolox treatment, western blot |
Proceedings of the National Academy of Sciences of the United States of America |
High |
37844241
|
| 2011 |
Interaction of the bluetongue virus NS3 N-terminal 13 residues with S100A10/p11 (demonstrated by pulldown and confocal microscopy) is essential for intracellular trafficking and plasma membrane egress of BTV in mammalian cells; NS3A mutants lacking this region fail to interact with S100A10/p11 and show severely attenuated growth despite normal protein expression, replication, dsRNA synthesis, and particle assembly. |
Reverse genetics, pulldown assay, confocal microscopy, site-directed mutagenesis |
Journal of virology |
Medium |
21411520
|
| 2023 |
S100A10 is secreted by HCC cells into extracellular vesicles (EVs) and governs protein cargoes in EVs by physically binding integrin αV, mediating association of MMP2, fibronectin, and EGF to EV membranes; EV-S100A10 upregulates EGFR, AKT, and ERK signaling and promotes HCC stemness and metastasis. |
Co-immunoprecipitation (S100A10-integrin αV), EV isolation and proteomic analysis, neutralizing antibody, siRNA knockdown, in vivo xenograft |
Gut |
Medium |
36631249
|
| 2008 |
The cAMP/PKA/CnA signaling axis regulates annexin 2-S100A10 complex formation and its interaction with TRPV6 in airway (16HBE14o-) and gut (Caco-2) epithelial cells; forskolin-stimulated complex formation was attenuated by PKA or calcineurin A inhibitors, and complex association with TRPV6 depended on CnA-dependent dephosphorylation of annexin 2. PKA and CnA inhibitors attenuated Ca2+ uptake in Caco-2 cells. |
Co-immunoprecipitation, calcium uptake assay, pharmacological inhibitors (PKA, CnA inhibitors), forskolin stimulation |
Cell calcium |
Medium |
18187190
|