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  • 1
    Online Resource
    Online Resource
    The Annexin 2/S100A10 Complex Controls the Distribution of Transferrin Receptor-containing Recycling Endosomes
    American Society for Cell Biology (ASCB) ; 2003
    In:  Molecular Biology of the Cell Vol. 14, No. 12 ( 2003-12), p. 4896-4908
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 14, No. 12 ( 2003-12), p. 4896-4908
    Abstract: The Ca 2+ - and lipid-binding protein annexin 2, which resides in a tight heterotetrameric complex with the S100 protein S100A10 (p11), has been implicated in the structural organization and dynamics of endosomal membranes. To elucidate the function of annexin 2 and S100A10 in endosome organization and trafficking, we used RNA-mediated interference to specifically suppress annexin 2 and S100A10 expression. Down-regulation of both proteins perturbed the distribution of transferrin receptor- and rab11-positive recycling endosomes but did not affect uptake into sorting endosomes. The phenotype was highly specific and could be rescued by reexpression of the N-terminal annexin 2 domain or S100A10 in annexin 2- or S100A10-depleted cells, respectively. Whole-mount immunoelectron microscopy of the aberrantly localized recycling endosomes in annexin 2/S100A10 down-regulated cells revealed extensively bent tubules and an increased number of endosome-associated clathrin-positive buds. Despite these morphological alterations, the kinetics of transferrin uptake and recycling was not affected to a significant extent, indicating that the proper positioning of recycling endosomes is not a rate-limiting step in transferrin recycling. The phenotype generated by this transient loss-of-protein approach shows for the first time that the annexin 2/S100A10 complex functions in the intracellular positioning of recycling endosomes and that both subunits are required for this activity.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e03-06-0387
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2003
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  • 2
    Online Resource
    Online Resource
    Ca 2+ -dependent Binding and Activation of Dormant Ezrin by Dimeric S100P
    American Society for Cell Biology (ASCB) ; 2003
    In:  Molecular Biology of the Cell Vol. 14, No. 6 ( 2003-06), p. 2372-2384
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 14, No. 6 ( 2003-06), p. 2372-2384
    Abstract: S100 proteins are EF hand type Ca 2 + binding proteins thought to function in stimulus-response coupling by binding to and thereby regulating cellular targets in a Ca 2 + -dependent manner. To isolate such target(s) of the S100P protein we devised an affinity chromatography approach that selects for S100 protein ligands requiring the biologically active S100 dimer for interaction. Hereby we identify ezrin, a membrane/F-actin cross-linking protein, as a dimer-specific S100P ligand. S100P-ezrin complex formation is Ca 2 + dependent and most likely occurs within cells because both proteins colocalize at the plasma membrane after growth factor or Ca 2 + ionophore stimulation. The S100P binding site is located in the N-terminal domain of ezrin and is accessible for interaction in dormant ezrin, in which binding sites for F-actin and transmembrane proteins are masked through an association between the N- and C-terminal domains. Interestingly, S100P binding unmasks the F-actin binding site, thereby at least partially activating the ezrin molecule. This identifies S100P as a novel activator of ezrin and indicates that activation of ezrin's cross-linking function can occur directly in response to Ca 2 + transients.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e02-09-0553
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2003
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  • 3
    Online Resource
    Online Resource
    The Formation of the cAMP/Protein Kinase A-dependent Annexin 2–S100A10 Complex with Cystic Fibrosis Conductance Regulator Protein (CFTR) Regulates CFTR Channel Function
    American Society for Cell Biology (ASCB) ; 2007
    In:  Molecular Biology of the Cell Vol. 18, No. 9 ( 2007-09), p. 3388-3397
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 18, No. 9 ( 2007-09), p. 3388-3397
    Abstract: Cystic fibrosis results from mutations in the cystic fibrosis conductance regulator protein (CFTR), a cAMP/protein kinase A (PKA) and ATP-regulated Cl − channel. CFTR is increasingly recognized as a component of multiprotein complexes and although several inhibitory proteins to CFTR have been identified, protein complexes that stimulate CFTR function remain less well characterized. We report that annexin 2 (anx 2)–S100A10 forms a functional cAMP/PKA/calcineurin (CaN)-dependent complex with CFTR. Cell stimulation with forskolin/3-isobutyl-1-methylxanthine significantly increases the amount of anx 2–S100A10 that reciprocally coimmunoprecipitates with cell surface CFTR and calyculin A. Preinhibition with PKA or CaN inhibitors attenuates the interaction. Furthermore, we find that the acetylated peptide (STVHEILCKLSLEG, Ac1-14), but not the nonacetylated equivalent N1-14, corresponding to the S100A10 binding site on anx 2, disrupts the anx 2–S100A10/CFTR complex. Analysis of 4,4′-diisothiocyanatostilbene-2,2′-disulfonic acid (DIDS) and CFTR inh172 -sensitive currents, taken as indication of the outwardly rectifying Cl − channels (ORCC) and CFTR-mediated currents, respectively, showed that Ac1-14, but not N1-14, inhibits both the cAMP/PKA-dependent ORCC and CFTR activities. CaN inhibitors (cypermethrin, cyclosporin A) discriminated between ORCC/CFTR by inhibiting the CFTR inh172 -, but not the DIDS-sensitive currents, by 〉 70%. Furthermore, peptide Ac1-14 inhibited acetylcholine-induced short-circuit current measured across a sheet of intact intestinal biopsy. Our data suggests that the anx 2–S100A10/CFTR complex is important for CFTR function across epithelia.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e07-02-0126
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2007
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  • 4
    Online Resource
    Online Resource
    A novel Munc13-4/S100A10/annexin A2 complex promotes Weibel–Palade body exocytosis in endothelial cells
    American Society for Cell Biology (ASCB) ; 2017
    In:  Molecular Biology of the Cell Vol. 28, No. 12 ( 2017-06-15), p. 1688-1700
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 28, No. 12 ( 2017-06-15), p. 1688-1700
    Abstract: Endothelial cells respond to blood vessel injury by the acute release of the procoagulant von Willebrand factor, which is stored in unique secretory granules called Weibel–Palade bodies (WPBs). Stimulated WPB exocytosis critically depends on their proper recruitment to the plasma membrane, but factors involved in WPB–plasma membrane tethering are not known. Here we identify Munc13-4, a protein mutated in familial hemophagocytic lymphohistiocytosis 3, as a WPB-tethering factor. Munc13-4 promotes histamine-evoked WPB exocytosis and is present on WPBs, and secretagogue stimulation triggers an increased recruitment of Munc13-4 to WPBs and a clustering of Munc13-4 at sites of WPB–plasma membrane contact. We also identify the S100A10 subunit of the annexin A2 (AnxA2)-S100A10 protein complex as a novel Munc13-4 interactor and show that AnxA2-S100A10 participates in recruiting Munc13-4 to WPB fusion sites. These findings indicate that Munc13-4 supports acute WPB exocytosis by tethering WPBs to the plasma membrane via AnxA2-S100A10.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e17-02-0128
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2017
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  • 5
    Online Resource
    Online Resource
    Tetraspanin CD9 links junctional adhesion molecule-A to αvβ3 integrin to mediate basic fibroblast growth factor–specific angiogenic signaling
    American Society for Cell Biology (ASCB) ; 2013
    In:  Molecular Biology of the Cell Vol. 24, No. 7 ( 2013-04), p. 933-944
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 24, No. 7 ( 2013-04), p. 933-944
    Abstract: Junctional adhesion molecule-A (JAM-A) is a member of the immunoglobulin family with diverse functions in epithelial cells, including cell migration, cell contact maturation, and tight junction formation. In endothelial cells, JAM-A has been implicated in basic fibroblast growth factor (bFGF)-regulated angiogenesis through incompletely understood mechanisms. In this paper, we identify tetraspanin CD9 as novel binding partner for JAM-A in endothelial cells. CD9 acts as scaffold and assembles a ternary JAM-A-CD9-αvβ3 integrin complex from which JAM-A is released upon bFGF stimulation. CD9 interacts predominantly with monomeric JAM-A, which suggests that bFGF induces signaling by triggering JAM-A dimerization. Among the two vitronectin receptors, αvβ3 and αvβ5 integrin, which have been shown to cooperate during angiogenic signaling with bFGF and vascular endothelial growth factor (VEGF), respectively, CD9 links JAM-A specifically to αvβ3 integrin. In line with this, knockdown of CD9 blocks bFGF- but not VEGF-induced ERK1/2 activation. JAM-A or CD9 knockdown impairs endothelial cell migration and tube formation. Our findings indicate that CD9 incorporates monomeric JAM-A into a complex with αvβ3 integrin, which responds to bFGF stimulation by JAM-A release to regulate mitogen-activated protein kinase (MAPK) activation, endothelial cell migration, and angiogenesis. The data also provide new mechanistic insights into the cooperativity between bFGF and αvβ3 integrin during angiogenic signaling.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e12-06-0481
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2013
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  • 6
    Online Resource
    Online Resource
    VE-cadherin interacts with cell polarity protein Pals1 to regulate vascular lumen formation
    American Society for Cell Biology (ASCB) ; 2016
    In:  Molecular Biology of the Cell Vol. 27, No. 18 ( 2016-09-15), p. 2811-2821
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 27, No. 18 ( 2016-09-15), p. 2811-2821
    Abstract: Blood vessel tubulogenesis requires the formation of stable cell-to-cell contacts and the establishment of apicobasal polarity of vascular endothelial cells. Cell polarity is regulated by highly conserved cell polarity protein complexes such as the Par3-aPKC-Par6 complex and the CRB3-Pals1-PATJ complex, which are expressed by many different cell types and regulate various aspects of cell polarity. Here we describe a functional interaction of VE-cadherin with the cell polarity protein Pals1. Pals1 directly interacts with VE-cadherin through a membrane-proximal motif in the cytoplasmic domain of VE-cadherin. VE-cadherin clusters Pals1 at cell–cell junctions. Mutating the Pals1-binding motif in VE-cadherin abrogates the ability of VE-cadherin to regulate apicobasal polarity and vascular lumen formation. In a similar way, deletion of the Par3-binding motif at the C-terminus of VE-cadherin impairs apicobasal polarity and vascular lumen formation. Our findings indicate that the biological activity of VE-cadherin in regulating endothelial polarity and vascular lumen formation is mediated through its interaction with the two cell polarity proteins Pals1 and Par3.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e16-02-0127
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2016
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  • 7
    Online Resource
    Online Resource
    Annexin 2 Promotes the Formation of Lipid Microdomains Required for Calcium-regulated Exocytosis of Dense-Core Vesicles
    American Society for Cell Biology (ASCB) ; 2005
    In:  Molecular Biology of the Cell Vol. 16, No. 3 ( 2005-03), p. 1108-1119
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 16, No. 3 ( 2005-03), p. 1108-1119
    Abstract: Annexin 2 is a calcium-dependent phospholipid-binding protein that has been implicated in a number of membranerelated events, including regulated exocytosis. In chromaffin cells, we previously reported that catecholamine secretion requires the translocation and formation of the annexin 2 tetramer near the exocytotic sites. Here, to obtain direct evidence for a role of annexin 2 in exocytosis, we modified its expression level in chromaffin cells by using the Semliki Forest virus expression system. Using a real-time assay for individual cells, we found that the reduction of cytosolic annexin 2, and the consequent decrease of annexin 2 tetramer at the cell periphery, strongly inhibited exocytosis, most likely at an early stage before membrane fusion. Secretion also was severely impaired in cells expressing a chimera that sequestered annexin 2 into cytosolic aggregates. Moreover, we demonstrate that secretagogue-evoked stimulation triggers the formation of lipid rafts in the plasma membrane, essential for exocytosis, and which can be attributed to the annexin 2 tetramer. We propose that annexin 2 acts as a calcium-dependent promoter of lipid microdomains required for structural and spatial organization of the exocytotic machinery.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e04-07-0627
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2005
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  • 8
    Online Resource
    Online Resource
    Annexin A8 Regulates Late Endosome Organization and Function
    American Society for Cell Biology (ASCB) ; 2008
    In:  Molecular Biology of the Cell Vol. 19, No. 12 ( 2008-12), p. 5267-5278
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 19, No. 12 ( 2008-12), p. 5267-5278
    Abstract: Different classes of endosomes exhibit a characteristic intracellular steady-state distribution governed by interactions with the cytoskeleton. Late endosomes, organelles of the degradative lysosomal route, seem to require associated actin filaments for proper localization and function. We show here that the F-actin and phospholipid binding protein annexin A8 is associated specifically with late endosomes. Altering intracellular annexin A8 levels drastically affected the morphology and intracellular distribution of late endosomes. Trafficking through the degradative pathway was delayed in the absence of annexin A8, resulting in attenuated ligand-induced degradation of the epidermal growth factor receptor and prolonged epidermal growth factor-induced activation of mitogen-activated protein kinase. Depletion of annexin A8 reduced the association of late endosomal membranes with actin filaments. These results indicate that the defective cargo transport through the late endocytic pathway and the imbalanced signaling of activated receptors observed in the absence of annexin A8 results from the disturbed association of late endosomal membranes with the actin network, resulting in impaired actin-based late endosome motility.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e08-04-0383
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2008
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