The ability of AIF-1 to activate human vascular smooth muscle cells is lost by mutations in the EF-hand calcium-binding region

Autieri, Michael V.; Chen, Xing

doi:10.1016/j.yexcr.2005.03.002

Cited by 18 publications

(13 citation statements)

References 41 publications

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“…S2b). EFhd2 exhibits F-actin bundling activity in a Ca 2+ -dependent manner, whereas AIF-1 does not exhibit Ca 2+ dependency for F-actin binding and bundling activity26323334.…”

Section: Resultsmentioning

confidence: 97%

Structural implications of Ca2+-dependent actin-bundling function of human EFhd2/Swiprosin-1

Park

Kwon

et al. 2016

Sci Rep

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EFhd2/Swiprosin-1 is a cytoskeletal Ca2+-binding protein implicated in Ca2+-dependent cell spreading and migration in epithelial cells. EFhd2 domain architecture includes an N-terminal disordered region, a PxxP motif, two EF-hands, a ligand mimic helix and a C-terminal coiled-coil domain. We reported previously that EFhd2 displays F-actin bundling activity in the presence of Ca2+ and this activity depends on the coiled-coil domain and direct interaction of the EFhd2 core region. However, the molecular mechanism for the regulation of F-actin binding and bundling by EFhd2 is unknown. Here, the Ca2+-bound crystal structure of the EFhd2 core region is presented and structures of mutants defective for Ca2+-binding are also described. These structures and biochemical analyses reveal that the F-actin bundling activity of EFhd2 depends on the structural rigidity of F-actin binding sites conferred by binding of the EF-hands to Ca2+. In the absence of Ca2+, the EFhd2 core region exhibits local conformational flexibility around the EF-hand domain and C-terminal linker, which retains F-actin binding activity but loses the ability to bundle F-actin. In addition, we establish that dimerisation of EFhd2 via the C-terminal coiled-coil domain, which is necessary for F-actin bundling, occurs through the parallel coiled-coil interaction.

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“…S2b). EFhd2 exhibits F-actin bundling activity in a Ca 2+ -dependent manner, whereas AIF-1 does not exhibit Ca 2+ dependency for F-actin binding and bundling activity26323334.…”

Section: Resultsmentioning

confidence: 97%

Structural implications of Ca2+-dependent actin-bundling function of human EFhd2/Swiprosin-1

Park

Kwon

et al. 2016

Sci Rep

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“…AIF-1, which was first discovered in rat cardiac allografts undergoing chronic rejection, has thus homologs in vertebrates and lower invertebrates [47]. In higher animals it plays a role in vascular remodelling and repair which probably involves induction of actin polymerisation in vascular smooth muscle cells and is dependent on an intact EF-hand motif [48,49]. The discovery of these two new 14-3-3 target proteins suggests a broader role of 14-3-3 proteins in Ca 2+ signalling.…”

Section: Resultsmentioning

confidence: 99%

Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca2+ signalling

et al. 2007

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Background: 14-3-3 proteins have been implicated in many signalling mechanisms due to their interaction with Ser/Thr phosphorylated target proteins. They are evolutionarily well conserved in eukaryotic organisms from single celled protozoans and unicellular algae to plants and humans. A diverse array of target proteins has been found in higher plants and in human cell lines including proteins involved in cellular metabolism, apoptosis, cytoskeletal organisation, secretion and Ca 2+ signalling.

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“…To define a possible role of calcium in the structure and/or activity of AtPXG1, we have modified the EFhand domain of AtPGX1 by site-directed mutagenesis. It was shown that mutation of the first amino acid of the EF-hand loop, an Asp coordinating Ca 2ϩ , abrogates calcium binding by AIF-1 and Tsc (41,42). On this basis, we replaced the Asp at position X of the EF-hand with Val as shown by the arrow in Fig.…”

Section: Expression Of Caleosins In Yeast and Identification As Plantmentioning

confidence: 99%

Plant Seed Peroxygenase Is an Original Heme-oxygenase with an EF-hand Calcium Binding Motif

Hanano

Burcklen

Flénet

et al. 2006

Journal of Biological Chemistry

136

167

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A growing body of evidence indicates that phytooxylipins play important roles in plant defense responses. However, many enzymes involved in the biosynthesis of these metabolites are still elusive. We have purified one of these enzymes, the peroxygenase (PXG), from oat microsomes and lipid droplets. It is an integral membrane protein requiring detergent for its solubilization. Proteinase K digestion showed that PXG is probably deeply buried in lipid droplets or microsomes with only about 2 kDa at the C-terminal region accessible to proteolytic digestion. Sequencing of the N terminus of the purified protein showed that PXG had no sequence similarity with either a peroxidase or a cytochrome P450 but, rather, with caleosins, i.e. calcium-binding proteins. In agreement with this finding, we demonstrated that recombinant thale cress and rice caleosins, expressed in yeast, catalyze hydroperoxide-dependent mono-oxygenation reactions that are characteristic of PXG. Calcium was also found to be crucial for peroxygenase activity, whereas phosphorylation of the protein had no impact on catalysis. Site-directed mutagenesis studies revealed that PXG catalytic activity is dependent on two highly conserved histidines, the 9 GHz EPR spectrum being consistent with a high spin pentacoordinated ferric heme.

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The ability of AIF-1 to activate human vascular smooth muscle cells is lost by mutations in the EF-hand calcium-binding region

Cited by 18 publications

References 41 publications

Structural implications of Ca2+-dependent actin-bundling function of human EFhd2/Swiprosin-1

Structural implications of Ca2+-dependent actin-bundling function of human EFhd2/Swiprosin-1

Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca2+ signalling

Plant Seed Peroxygenase Is an Original Heme-oxygenase with an EF-hand Calcium Binding Motif

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