Surface Topography of the p3 and p6 Annexin V Crystal Forms Determined by Atomic Force Microscopy

Reviakine, Ilya; Bergsma-Schutter, Wilma; Mazères-Dubut, Christine; Govorukhina, Natalia; Brisson, Alain

doi:10.1006/jsbi.2000.4286

Cited by 76 publications

(81 citation statements)

References 26 publications

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“…In constructing this figure, we also consider a published crystal structure of annexin A5 in complex with Ca 2ϩ , and glycerophosphoserine, an analogue of the polar head-group of phosphatidylserine (8). Based on this annexin A5 structure, we modeled Ca 2ϩ (yellow) and PO 4 (green and red) into annexin B12 in Fig. 5, right, which represents the membrane-bound form of the protein.…”

Section: Discussionmentioning

confidence: 99%

“…5, right, which represents the membrane-bound form of the protein. The Ca 2ϩ and PO 4 provide orientation with regard to the location of the bilayer, which would be expected to be horizontal and below the protein in Fig. 5.…”

Section: Discussionmentioning

confidence: 99%

“…Despite its obvious biological importance, relatively little detailed molecular information is available regarding the structure and dynamics of the membrane-bound form of the annexins. Images of two-dimensional crystals of annexins 4 and 5 on phospholipid monolayers obtained by electron crystallography indicated that the membrane-bound proteins had the same general shape as observed in x-ray crystal studies of the soluble proteins but lacked the resolution to draw further inferences (2, 3) Atomic force microscopy studies of annexin A5 on the surface of planar lipid bilayers reached similar conclusions (4).…”

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confidence: 87%

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Structure and Dynamics of a Helical Hairpin that Mediates Calcium-dependent Membrane Binding of Annexin B12

Isas

Langen

Hubbell

et al. 2004

Journal of Biological Chemistry

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A wealth of high-resolution structural data has accumulated for soluble annexins, but only limited information is available for the biologically important membrane-bound proteins. To investigate the structural and dynamic changes that occur upon membrane binding, we analyzed the electron paramagnetic resonance (EPR) mobility and accessibility parameters of a contin- showed that the overall backbone fold for the scanned region did not change upon membrane binding. However, side-chains in the loop between the D and E helices were highly dynamic in solution but became essentially frozen in the EPR time scale upon binding to membranes. Accessibility measurements clearly established that side-chains in this loop were exposed to the hydrophobic core of the bilayer and provide the first evidence that a D-E loop directly participates in the Ca 2؉ -dependent binding of annexins to membranes. Other localized changes showed that the D-helix became much less dynamic after membrane binding and identified quaternary contact sites in the membrane-bound homo-trimer. Finally, immobilization of the D-E loop upon contact with phospholipid suggests that the bilayer, which is normally very mobile on the EPR time scale, is immobilized in the head-group region by the annexin B12. This suggests that annexin B12 alters membrane structure in a manner that may be biologically significant.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 87%

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Structure and Dynamics of a Helical Hairpin that Mediates Calcium-dependent Membrane Binding of Annexin B12

Isas

Langen

Hubbell

et al. 2004

Journal of Biological Chemistry

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“…This could allow them to organize the interface between the cytoplasm (or cytoskeleton) and the cytoplasmic face of cellular membranes. In fact, cryoelectron and atomic force microscopy of annexins bound to model membranes have provided compelling images of the proteins forming two-dimensional lattices or certain domains on the surface of membranes (Janshoff et al, 2001;Lambert et al, 1997;Reviakine et al, 2000;Lambert et al, 2004). Although the coating of target membranes to establish and/or regulate lateral membrane domains is likely to be a key element of annexin function, a few questions remain.…”

Section: Annexins As Membrane Scaffold Proteinsmentioning

confidence: 99%

Annexins – unique membrane binding proteins with diverse functions

Rescher

Gerke

2004

Journal of Cell Science

540

435

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IntroductionThe annexins are a family of Ca 2+ /lipid-binding proteins that differ from most other Ca 2+ -binding proteins in their Ca 2+ -binding sites. These have a unique architecture that allows them to dock onto membranes in a peripheral and reversible manner. The conserved Ca 2+ -and membrane-binding module is the annexin core domain, which consists of four so-called annexin repeats, each of which is 70 residues in length. It is highly α-helical and forms a compact, slightly curved disc that has a convex surface harboring the Ca 2+ -and membranebinding sites and a concave side that points away from the membrane and is thereby available for other types of interaction/regulation (Fig. 1). The N-terminal region precedes the core domain and is diverse in sequence and length. It mediates regulatory interactions with protein ligands and regulates the annexin-membrane association (reviewed by Gerke and Moss, 2002;Raynal and Pollard, 1994). Although the N-terminal domain has long been considered a separately folded entity, recent crystal structures reveal that, at least in annexin A1, part of it can integrate into the folded core. Ca 2+ (and probably membrane) binding can then trigger exposure of the N-terminal region, making it available for additional interactions/activities ( Fig. 1) (Rosengarth and Luecke, 2003). The activity of the exposed N-terminal region could thus be tightly controlled through Ca 2+ /membrane binding.The annexin family comprises >500 different gene products expressed in most phyla and species (reviewed by Morgan and Fernandez, 1997). In vertebrates, 12 annexin subfamilies (A1-A11 and A13), which have different splice variants, have been identified. These have different N-terminal domains and differently positioned Ca 2+ /membrane-binding sites within the core domain. Analyses of the biochemical properties and subcellular localizations of annexins, and later studies of the effects of anti-annexin antibodies and annexin mutants, mainly in permeabilized cell systems, have allowed several potential physiological functions to be assigned to different annexins. Most of these take into account their regulated binding to membranes and a scaffold role at certain membrane domains is a common theme.Proposed to act as membrane-membrane or membranecytoskeleton linkers, annexins have been implicated in Ca 2+ -regulated exocytotic events, certain aspects of endocytosis and stabilization of specific domains of organelle membranes and the plasma membrane. However, other potential functions have been put forward -for example, those taking into account the RNA-binding capacity of some annexins (Filipenko et al., 2004;Vedeler and Hollas, 2000), their regulated nuclear localization (Eberhard et al., 2001;Mizutani et al., 1992;Tomas and Moss, 2003) or specific nucleotide-binding activities (Banderowicz-Pikula et al., 2001; Caohuy et al., 1996). Because some annexins occur extracellularly, they might also function outside the cell, although their (direct or indirect) secretion is not well understood. Detailed ...

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“…The single cysteine residue of Anx5-SH was stereo-selectively inserted in a solventexposed loop on the concave face of Anx5, opposite to the membrane-binding face, in order to ensure high accessibility of the coupled elements. 54,55 The Anx5-RGD and Anx5-IKVAV disulfide-linked complexes were produced at close to 100% purity with an overall yield of 20% ͑data not shown͒. Molecular masses of 36 738 and 37 608 Da were determined by MALDI-TOF mass spec- …”

Section: A Synthesis Of Anx5-peptide Complexesmentioning

confidence: 99%

Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: An efficient platform for cell adhesion

et al. 2007

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Understanding and controlling cell adhesion to biomaterials and synthetic materials are important issues in basic research and applied sciences. Supported lipid bilayers ͑SLBs͒ functionalized with cell adhesion peptides linked to lipid molecules are popular platforms of cell adhesion. In this paper, an alternative approach of peptide presentation is presented in which peptides are stereo-selectively linked to proteins self-assembling in a rigid two-dimensional ͑2D͒ matrix on SLBs. Annexin-A5 ͑Anx5͒ was used as prototype protein for its known properties of forming stable and rigid 2D matrices on lipid surfaces. Two types of Anx5-peptide complexes, containing either a RGD or an IKVAV sequence, were synthesized. The authors show that both Anx5-peptide complexes present the same properties of binding and 2D organization on lipid surfaces as Anx5, when investigated by quartz crystal microbalance with dissipation monitoring, atomic force microscopy, and transmission electron microscopy techniques. Anx5-RGD and Anx5-IKVAV 2D matrices were found to promote specific adhesion of human saphenous vein endothelial cells and mouse embryonic stem cells, respectively. The influence of the surface density of exposed peptides on cell adhesion was investigated, showing that cells attach to Anx5-peptide matrices when the average distance between peptides is smaller than about 60 nm. This cell adhesion platform provides control of the orientation and density of cell ligands, opening interesting possibilities for future applications.

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Surface Topography of the p3 and p6 Annexin V Crystal Forms Determined by Atomic Force Microscopy

Cited by 76 publications

References 26 publications

Structure and Dynamics of a Helical Hairpin that Mediates Calcium-dependent Membrane Binding of Annexin B12

Structure and Dynamics of a Helical Hairpin that Mediates Calcium-dependent Membrane Binding of Annexin B12

Annexins – unique membrane binding proteins with diverse functions

Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: An efficient platform for cell adhesion

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