Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study

Buzhynskyy, Nikolay; Golczak, Marcin; Lai-Kee-Him, Joséphine; Lambert, Olivier; Tessier, Béatrice; Gounou, Céline; Bérat, Rémi; Simon, Anne; Granier, T.; Chevalier, J.‐M.; Mazères, Serge; Bandorowicz‐Pikuła, Joanna; Pikula, Sławomir; Brisson, Alain

doi:10.1016/j.jsb.2009.03.007

Cited by 47 publications

(35 citation statements)

References 55 publications

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“…As described in more detail in recent reviews from our laboratories (20,27), AnxA6 interacts with a large number of signalling proteins and members of the actin cytoskeleton (see Table 1 for selected interaction partners). Together with its lipid binding affinity, this suggests that AnxA6 may organize membrane domains to create a scaffold for the formation and spatio-temporal regulation of multifactorial signalling complexes possibly involving transient membrane-actin interactions (27,29).…”

Section: The Annexin Familymentioning

confidence: 99%

Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling

et al. 2011

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Annexin A6 (AnxA6) belongs to the conserved annexin protein family—a group of Ca2+‐dependent membrane binding proteins. It is the largest of all annexin proteins and upon activation, binds to negatively charged phospholipids in the plasma membrane and endosomes. In addition, AnxA6 associates with cholesterol‐rich membrane microdomains termed lipid rafts. Membrane cholesterol triggers Ca2+‐independent translocation of AnxA6 to membranes and AnxA6 levels determine the number of caveolae, a form of specialized rafts at the cell surface. AnxA6 also has an F‐actin binding domain and interacts with cytoskeleton components. Taken together, this suggests that AnxA6 has a scaffold function to link membrane microdomains with the organization of the cytoskeleton. Such a link facilitates AnxA6 to participate in plasma membrane repair and it would also impact on receptor signalling at the cell surface, growth factor, and lipoprotein receptor trafficking, Ca2+‐channel activity and T cell activation. Hence, the regulation of cell surface receptors by AnxA6 may be facilitated by its unique structure that allows recruitment of interaction partners and simultaneously bridging specialized membrane domains with cortical actin surrounding activated receptors. © 2011 IUBMB IUBMB Life, 63(11): 1009–1017, 2011

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Section: The Annexin Familymentioning

confidence: 99%

Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling

et al. 2011

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“…Due to the presence of the flexible linker region AnxA6-1 may exhibit two modes of association with lipid membranes depending on calcium concentration. Studies on the membranebound AnxA6-1 showed that the two annexin modules reorient during membrane binding [16,18]. Thus, the AnxA6 flexible region with Trp343 residue seems to play crucial role in its interaction with membranes and may also regulate its behavior in solution.…”

Section: Introductionmentioning

confidence: 99%

Interaction of annexin A6 with cholesterol rich membranes is pH-dependent and mediated by the sterol OH

Domon

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Strzelecka‐Kiliszek

et al. 2010

Journal of Colloid and Interface Science

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“…Atomic force microscopy, due to its very high S/N ratio, is a promising alternative technique. Establishing a relationship between atomic coordinates and AFM topographic images has already illustrated (Asakawa et al, 2011; Buzhynskyy et al, 2009; Czajkowsky et al, 2004; Czajkowsky and Shao, 2009; Davies et al, 2005; Philippsen et al, 2002; Scheuring et al, 2007; Scheuring et al, 2005). In this work we use, for the first time, AFM topography as low-resolution envelopes into which we place atomic coordinates using the rigid body protein docking program DOT (Mandell et al, 2001; Ten Eyck et al, 1995).…”

Section: Introductionmentioning

confidence: 88%

Computational Reconstruction of Multidomain Proteins Using Atomic Force Microscopy Data

et al. 2012

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Summary Classical structural biology techniques face a great challenge to determine the structure at the atomic level of large and flexible macromolecules. We present a novel methodology that combines high-resolution AFM topographic images with atomic coordinates of proteins to assemble very large macromolecules or particles. Our method uses a two-step protocol: atomic coordinates of individual domains are docked beneath the molecular surface of the large macromolecule, and then each domain is assembled using a combinatorial search. The protocol was validated on three test cases: a simulated system of antibody structures; and two experimentally-based test cases: Tobacco mosaic virus, a rod-shaped virus; and aquaporin Z, a bacterial membrane protein. We have shown that AFM-intermediate resolution topography and partial surface data are useful constraints for building macromolecular assemblies. The protocol is applicable to multi-component structures connected in the polypeptide chain or as disjoint molecules. The approach effectively increases the resolution of AFM beyond topographical information down to atomic-detail structures.

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Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study

Cited by 47 publications

References 55 publications

Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling

Annexin A6 is an organizer of membrane microdomains to regulate receptor localization and signalling

Interaction of annexin A6 with cholesterol rich membranes is pH-dependent and mediated by the sterol OH

Computational Reconstruction of Multidomain Proteins Using Atomic Force Microscopy Data

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