Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I

Fuente, Milton De La; Ossa, Carmen Gloria

doi:10.1016/s0006-3495(97)78677-6

Cited by 21 publications

(19 citation statements)

References 25 publications

(23 reference statements)

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“…Proteolysis of annexin 1 bound to phosphatidylserine-vesicles was almost complete after one minute, whereas about 30 minutes were required to cleave annexin 1 in solution. 17,19 Combining the results from these publications, it seems likely that annexin 1 binds to membranes containing negatively charged phospholipids first. This binding event is calcium-dependent, and involves the convex site of the molecule using calcium ions as bridges between the annexin and the bilayer.…”

Section: Membrane Interaction Of the Annexin 1 N-terminal Domainmentioning

confidence: 84%

“…Interestingly, this secondary binding site exhibits neither calcium dependency nor lipid specificity. 9,13,[18][19][20] These data suggest that the N-terminal domain of annexin 1 alone might provide a second membrane-binding site. This hypothesis is supported by a publication from Lee and co-workers in which they present data that a peptide comprising residues 1-26 of annexin 1 alone is able to form an α-helix in 50% trifluorethanol (TFE)/water and 10 mM sodium dodecyl sulfate (SDS), suggesting membrane binding activity.…”

Section: +mentioning

confidence: 99%

“…19,33 It has been shown that membrane-bound annexin 1 is approximately 40 times more sensitive to trypsin (which cleaves at position Lys26) and cathepsin D (which cleaves at residue 12) than free annexin 1. 19 Therefore, the N-terminal domain of annexin 1 is more accessible as a result of calcium-dependent membrane binding than in the calcium-free from. These results are in good agreement with our hypothesis that the helix NA is only accessible after calcium and/or membrane binding.…”

Section: The Structure Of Full-length Annexin 1 In the Presence Of Camentioning

confidence: 99%

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A Calcium-driven Conformational Switch of the N-terminal and Core Domains of Annexin A1

Rosengarth

Luecke

2003

Journal of Molecular Biology

125

118

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A nnexins are structurally divided into a highly conserved core domain and a variable N-terminal domain. The core domain mediates the calcium-dependent phospholipid binding of annexins, whereas the N-terminal domain, which is unique in sequence and length for each member of this protein family, is responsible for the specificity among the different members. Annexin 1 has been shown to possess membrane aggregation and fusion activity in the presence of calcium in vitro. Due to the high sequence homology of the core domain among different annexins, the property of membrane aggregation has been attributed to the N-terminal domain. For instance, a chimera protein comprising the core of annexin 5, which by itself does not exhibit membrane aggregation properties, and the N-terminal domain of annexin 1 is able to induce membrane aggregation. Numerous three-dimensional structures of annexins have been solved using x-ray crystallography, however, none reveal the tertiary structure of an N-terminal domain or its interaction with the core domain. We have solved the x-ray structure of full-length annexin 1 with an N-terminal domain comprising 42 amino acids in the absence of calcium ions at 1.8 Å resolution. Residues 2-26 of the N-terminal domain exhibit a mainly α-helical conformation with a kink at residue 17. Helix NA (residues 2 to 16) inserts into repeat III of the core domain thereby replacing the old helix D. Helix D on the other hand unfolds into an extended loop that forms a flap over the top of helix NA of the N-terminal domain. As a result, the type II calcium-binding site located in core repeat III is destroyed because the "capping residue" for calcium ion coordination is not in the proper conformation/location any more. Also presented in this article is the structure of full-length annexin 1 in the presence of 1 mM CaCl 2 . The structure of full-length annexin 1 in the absence of calcium ions is thought to represent the "inactive" form of the protein. We provide a model for the annexin 1-induced membrane aggregation and discuss it in light of the literature published to date.

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Section: Membrane Interaction Of the Annexin 1 N-terminal Domainmentioning

confidence: 84%

Section: +mentioning

confidence: 99%

Section: The Structure Of Full-length Annexin 1 In the Presence Of Camentioning

confidence: 99%

See 1 more Smart Citation

A Calcium-driven Conformational Switch of the N-terminal and Core Domains of Annexin A1

Rosengarth

Luecke

2003

Journal of Molecular Biology

125

118

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“…Previous studies on annexin I-induced membrane aggregation indicated the presence of an inducible secondary interaction site for membrane aggregation that is distinct from the primary membrane-binding site (19,28,29,35,36). Three major topological models of annexin I-mediated membrane aggregation, which are based on the presence of the inducible secondary interaction site, are depicted in Figure 1, panels a-c. Each model could also involve the lateral association of membrane-bound annexin molecules, as shown in Figure 1, panels d-f.…”

Section: Models Of Annexin I-induced Membrane Aggregationmentioning

confidence: 99%

Mechanism of Annexin I-Mediated Membrane Aggregation

Bitto

Tikhonov

et al. 2000

Biochemistry

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It has been proposed that annexin I has two separate interaction sites that are involved in membrane binding and aggregation, respectively. To better understand the mechanism of annexin I-mediated membrane aggregation, we investigated the properties of the inducible secondary interaction site implicated in membrane aggregation. X-ray specular reflectivity measurements showed that the thickness of annexin I layer bound to the phospholipid monolayer was 31 ( 2 Å, indicating that annexin I binds membranes as a protein monomer or monolayer. Surface plasmon resonance measurements of annexin I, V, and mutants, which allowed evaluation of membrane aggregation activity of annexin I separately from its membrane binding, revealed direct correlation between the relative membrane aggregation activity and the relative affinity of the secondary interaction site for the secondary membrane. The secondary binding was driven primarily by hydrophobic interactions, unlike calcium-mediated electrostatic primary membrane binding. Chemical cross-linking of membrane-bound annexin I showed that a significant degree of lateral association of annexin I molecules precedes its membrane aggregation. Taken together, these results support a hypothetical model of annexin I-mediated membrane aggregation, in which a laterally aggregated monolayer of membrane-bound annexin I directly interacts with a secondary membrane via its induced hydrophobic interaction site.

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“…9 The calcium-and membrane-binding sites are located on the convex face but additional phospholipid-binding sites have been described for the N-terminal domain located on the concave face (annexin A1). 10,11 The N-terminal domains of annexins are highly variable and confer specific properties to each particular annexin. The alpha-giardins have been classified as representatives of a new annexin subfamily (annexin E family) due to their low but significant sequence identity with annexins from other organisms, but to date no three dimensional structure has been determined for any alphagiardin.…”

Section: Introductionmentioning

confidence: 99%

Apo and Calcium-bound Crystal Structures of Alpha-11 Giardin, an Unusual Annexin from Giardia lamblia

Pathuri

Nguyen

Svärd

et al. 2007

Journal of Molecular Biology

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SummaryAlpha-11 giardin is a member of the multi-gene alpha giardin family in the intestinal protozoan, Giardia lamblia. This gene family shares an ancestry with the annexin super family, whose common characteristic is calcium-dependent binding to membranes that contain acidic phospholipids. Several alpha giardins are highly expressed during parasite-induced diarrhea in humans. Despite being a member of a large family of proteins, little is known about the function and cellular localization of alpha-11 giardin, although giardins are often associated with the cytoskeleton. It has been shown that Giardia exhibits high levels of alpha-11 giardin mRNA transcript throughout its life cycle; however, constitutive expression of this protein is lethal to the parasite. Determining the three-dimensional structure of an alpha giardin is essential to identifying functional domains shared in the alpha giardin family. Here we report the crystal structures of the apo and Ca 2+ -bound forms of alpha-11 giardin, the first alpha giardin to be characterized structurally. Crystals of apo and Ca 2+ -bound alpha-11 giardin diffracted to 1.1 Å and 2.93 Å, respectively. The crystal structure of selenium-substituted apo alpha-11 giardin reveals a planar array of four tandem repeats of predominantly α-helical domains, reminiscent of previously determined annexin structures, making this the highest-resolution structure of an annexin to date. The apo alpha-11 giardin structure also reveals a hydrophobic core formed between repeats I/IV and II/III, a region typically hydrophilic in other annexins. Surprisingly, the Ca 2+ -bound structure contains only a single calcium ion, located in the DE loop of repeat I and coordinated differently from the two types of calcium sites observed in previous annexin structures. The apo and Ca 2+ -bound alpha-11 giardin structures assume overall similar conformations; however, calcium-bound alpha-11 giardin crystallized in a lower-symmetry spacegroup with four molecules in the asymmetric unit. Vesicle-binding studies suggest that alpha-11 giardin, unlike most other annexins, does not bind to vesicles composed of acidic phospholipids in a calcium-dependent manner.

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Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I

Cited by 21 publications

References 25 publications

A Calcium-driven Conformational Switch of the N-terminal and Core Domains of Annexin A1

A Calcium-driven Conformational Switch of the N-terminal and Core Domains of Annexin A1

Mechanism of Annexin I-Mediated Membrane Aggregation

Apo and Calcium-bound Crystal Structures of Alpha-11 Giardin, an Unusual Annexin from Giardia lamblia

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