Mutation of Highly Conserved Arginine Residues Disrupts the Structure and Function of Annexin V

Campos, Begoña; Wang, Songtao; Retzinger, Gregory S.; Kaetzel, Marcia A.; Seaton, Barbara A.; Karin, Norman J.; Johnson, J D; Dedman, John R.

doi:10.1016/s0188-0128(99)00040-8

Cited by 8 publications

(6 citation statements)

References 32 publications

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“…Generally speaking, membrane-bound anxV varies with the calcium and protein concentrations as described in the "Results" section, which agrees with published work (Campos et al 1999;Cezanne et al 1999;Jin et al 2004;Ungethum et al 2011;Yen et al 2010). Calcium and anxV protein, which influence each other, are two key factors affecting membrane-bound anxV.…”

Section: Discussionsupporting

confidence: 89%

“…In addition to calcium concentration, the anxV-membrane (with exposed phospholipids) interaction is influenced by many other factors, such as the anxV concentration, protein/membrane ratio, phospholipid composition, and transmembrane voltage (Campos et al 1999;Meers and Mealy 1993;Montaville et al 2002;Smith et al 2009;Ungethum et al 2011). The anxV-membrane binding reaction is a complex event, involving phospholipid clustering and immobilization, protein clustering, alterations of membrane shape, and rigidity at high protein/membrane ratio (Andree et al 1992;Bouter et al 2011;Cezanne et al 1999;Tait et al 2004).…”

mentioning

confidence: 99%

“…Generally speaking, the concentration of membranebound anxV increases gradually as the calcium or anxV concentration increases (Campos et al 1999;Cezanne et al 1999;Jin et al 2004;Ungethum et al 2011;Yen et al 2010). Some models have been proposed and tested to explain this phenomenon, indicating that anxV-membrane binding is highly cooperative with respect to calcium and negatively correlated with the protein density on the membrane (Bazzi and Nelsestuen 1991;Tait et al 2004).…”

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confidence: 99%

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Quantitative analysis of annexin V–membrane interaction by flow cytometry

Wang

Chen

et al. 2015

Eur Biophys J

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We constructed a green fluorescent phosphatidylserine (PS)-binding probe, which was generated by fusing enhanced green fluorescent protein (EGFP) to the C terminus of human annexin V (anxV). With this probe, we investigated anxV-membrane interaction under different calcium and anxV-EGFP concentrations through flow cytometry (FCM). A mathematical description of the binding characteristics is proposed and validated to quantify the relationship concerning the relative concentration of membrane-bound anxV (B), calcium concentration ([C]), and protein concentration ([P]). Further analyses reveal that [Formula: see text] is linear with [Formula: see text] or [Formula: see text] when [P] and [C] are fixed, respectively, which indicates that the anxV-membrane binding reaction may involve sequential multiple steps. Our study provides a reference for application of anxV in apoptosis detection. The mathematical expression facilitates exploration of the possible interactions between calcium, anxV, and membrane. The corresponding mathematical analysis strengthens the interpretation of the interaction data.

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Section: Discussionsupporting

confidence: 89%

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confidence: 99%

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confidence: 99%

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Quantitative analysis of annexin V–membrane interaction by flow cytometry

Wang

Chen

et al. 2015

Eur Biophys J

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“…Studies on the C2 domain superfamily have indicated that there are differences in membrane‐binding aa residues found on the surface of these proteins that could account for functional and biochemical diversity within this protein family (Jiménez et al ., ; Zhang & Aravind, ). The importance of surface‐exposed basic and hydrophobic residues for phospholipid binding, especially in the calcium‐independent C2 subfamilies, finds clear analogy with annexin subfamilies where highly conserved Arg residues in all annexin domain B‐C loops determine the molecular conformation and membrane‐binding affinity (Campos et al ., ). An additional role for basic residues and conserved Trp residues adjacent to the type II calcium‐binding sites in annexin A5 (Mo et al ., ; Sopkova de Oliveira Santos et al ., ) can also be extended to equivalent structures observed in plant annexin domains 1 (e.g.…”

Section: Structural Analysesmentioning

confidence: 99%

Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles

et al. 2012

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Contents Summary695I.Introduction695II.Structural analyses696III.Membrane‐related functions702IV.Enzyme‐related functions703V.Functional insights from proteome and transcriptome analyses704VI.Future perspectives706Acknowledgements708References708 Summary Annexins are an homologous, structurally related superfamily of proteins known to associate with membrane lipid and cytoskeletal components. Their involvement in membrane organization, vesicle trafficking and signaling is fundamental to cellular processes such as growth, differentiation, secretion and repair. Annexins exist in some prokaryotes and all eukaryotic phyla within which plant annexins represent a monophyletic clade of homologs descended from green algae. Genomic, proteomic and transcriptomic approaches have provided data on the diversity, cellular localization and expression patterns of different plant annexins. The availability of 35 complete plant genomes has enabled systematic comparative analysis to determine phylogenetic relationships, characterize structures and observe functional specificity between and within individual subfamilies. Short amino termini and selective erosion of the canonical type 2 calcium coordinating sites in domains 2 and 3 are typical of plant annexins. The convergent evolution of alternate functional motifs such as ‘KGD’, redox‐sensitive Cys and hydrophobic Trp/Phe residues argues for their functional relevance and contribution to mechanistic diversity in plant annexins. This review examines recent findings and advances in plant annexin research with special focus on their structural diversity, cellular and molecular interactions and their potential integrated functions in the broader context of physiological responses.

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“…The presence of motif associated with fibrinolytic and anticoagulant activity of the annexins that are associated with the schistosome tegument membrane may indicate a strong role for these molecules in presenting coagulation in the blood stream [27]. Arginine residues, which are involved in structural stability of the annexin tertiary structure [11,73], were found to be conserved in repeats I, III and IV of the C-terminal core domain of S. mansoni annexins.…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Molecular characterization of Schistosoma mansoni tegument annexins and comparative analysis of antibody responses following parasite infection

Leow

Willis

Hofmann

et al. 2019

Molecular and Biochemical Parasitology

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Mutation of Highly Conserved Arginine Residues Disrupts the Structure and Function of Annexin V

Cited by 8 publications

References 32 publications

Quantitative analysis of annexin V–membrane interaction by flow cytometry

Quantitative analysis of annexin V–membrane interaction by flow cytometry

Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles

Molecular characterization of Schistosoma mansoni tegument annexins and comparative analysis of antibody responses following parasite infection

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