Evolutionary perspective on annexin calcium-binding domains

Morgan, Reginald O.; Martin-Almedina, Silvia; Iglesias, Juan Manuel; Gonzalez-Florez, M.I.; Fernández, Mónica

doi:10.1016/j.bbamcr.2004.09.010

Cited by 74 publications

(63 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…S1 and Table S1), although Archaea and Eukarya have significantly (P < 0.01) greater slopes than Bacteria. Large-scale expansions of Cabinding protein families have been reported in the larger eukaryotic proteomes (23), and the α >1 power-law scaling extends those trends to both akaryotic superkingdoms.…”

Section: Resultsmentioning

confidence: 66%

History of biological metal utilization inferred through phylogenomic analysis of protein structures

Dupont

Butcher

Valas³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

275

247

View full text Add to dashboard Cite

The fundamental chemistry of trace elements dictates the molecular speciation and reactivity both within cells and the environment at large. Using protein structure and comparative genomics, we elucidate several major influences this chemistry has had upon biology. All of life exhibits the same proteome size-dependent scaling for the number of metal-binding proteins within a proteome. This fundamental evolutionary constant shows that the selection of one element occurs at the exclusion of another, with the eschewal of Fe for Zn and Ca being a defining feature of eukaryotic proteomes. Early life lacked both the structures required to control intracellular metal concentrations and the metal-binding proteins that catalyze electron transport and redox transformations. The development of protein structures for metal homeostasis coincided with the emergence of metal-specific structures, which predominantly bound metals abundant in the Archean ocean. Potentially, this promoted the diversification of emerging lineages of Archaea and Bacteria through the establishment of biogeochemical cycles. In contrast, structures binding Cu and Zn evolved much later, providing further evidence that environmental availability influenced the selection of the elements. The late evolving Zn-binding proteins are fundamental to eukaryotic cellular biology, and Zn bioavailability may have been a limiting factor in eukaryotic evolution. The results presented here provide an evolutionary timeline based on genomic characteristics, and key hypotheses can be tested by alternative geochemical methods.Archean-Proterozoic | biogeochemistry | bioinorganic chemistry | evolution | metal homeostasis M etalloproteins contain one or more ions of an inorganic element in their 3D structure and are said to comprise 30% of all proteins (1). Many biological pathways contain at least one metalloenzyme (2) and consequently require Mg, K, Ca, Fe, Mn, and Zn to sustain life (3). Other elements, like Cu, Mo, Ni, Se, and Co, are required by many-though not all-organismal lineages, and the utilization of trace elements varies greatly between species (3). The different elements have a range of affinities for most coordinating environments in the order Mg +2 /Ca +2 < Mn +2 < Fe +2 < Co +2 < Ni +2 < Cu +2 ∼Zn +2 , an equilibrium series known as the Irving-Williams Series (4). This array of outer-sphere chemistry provides significant catalytic diversity, yet has consequences for both biological and environmental chemistry. Within the cell, metals compete for protein binding sites; hence, extensive protein networks involving transporters and metalsensing regulatory proteins are required to maintain the proper subcellular concentrations of each element, and in some cases directly shuttle each metal to its requisite metalloprotein in the proper cellular compartment (1, 5, 6). It has been hypothesized that the establishment of a metal homeostasis system is required for distinct phylotypes of cells to develop (7).Environmentally, for similar fundamental chemical reasons, the...

show abstract

Section: Resultsmentioning

confidence: 66%

History of biological metal utilization inferred through phylogenomic analysis of protein structures

Dupont

Butcher

Valas³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

275

247

View full text Add to dashboard Cite

show abstract

“…16,17,33,34 Our bioinformatic analysis showed that Eg-ANX has lost Ca 2+ -binding sites in repeats II and III, and this loss was Immunofluorescence localization of Eg-ANX in different stages of E. granulosus. Eg-ANX in the protoscolex, germinal layer, and adult was immunofluorescently labeled using specific anti-rEg-ANX IgG (positive), or control pre-immune serum (negative), followed by fluorescein isothiocyanate (FITC)-conjugated anti-rabbit IgG.…”

Section: Discussionmentioning

confidence: 86%

Characterization of a Secretory Annexin in Echinococcus granulosus

Song¹,

Hu²,

Zhong³

et al. 2016

The American Journal of Tropical Medicine and Hygiene

View full text Add to dashboard Cite

Abstract. Cystic echinococcosis, caused by Echinococcus granulosus, is a widespread parasitic zoonosis causing economic loss and public health problems. Annexins are important proteins usually present in the plasma membrane, but previous studies have shown that an annexin B33 protein of E. granulosus (Eg-ANX) could be detected in the excretory/ secretory products and cyst fluid. In this study, we cloned and characterized Eg-ANX. In silico analysis showed that the amino acid sequence of Eg-ANX was conserved and lacked any signal peptides. The phospholipid-binding activity of recombinant Eg-ANX (rEg-ANX) was tested; liposomes could bind to rEg-ANX only in the presence of Ca 2+

show abstract

“…This may point to a unique loss of function mutation in the calcium binding motifs of AnxA8 during evolution. Earlier studies on the evolution of annexin calcium-binding domains in annexins already raised the question about the functional relevance and physiological roles of modifications within these calcium binding domains (30). The differences in the recognition of the PS signal by individual annexins now links the structural conservation of the GXGTD-[X] 37 -(D/E) motif to annexinspecific roles in the recognition of apoptotic cells.…”

Section: Discussionmentioning

confidence: 99%

Identification of Novel Binding Partners (Annexins) for the Cell Death Signal Phosphatidylserine and Definition of Their Recognition Motif

Rosenbaum

Kreft

Etich

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Identification and clearance of apoptotic cells prevents the release of harmful cell contents thereby suppressing inflammation and autoimmune reactions. Highly conserved annexins may modulate the phagocytic cell removal by acting as bridging molecules to phosphatidylserine, a characteristic phagocytosis signal of dying cells. In this study five members of the structurally and functionally related annexin family were characterized for their capacity to interact with phosphatidylserine and dying cells. The results showed that AnxA3, AnxA4, AnxA13, and the already described interaction partner AnxA5 can bind to phosphatidylserine and apoptotic cells, whereas AnxA8 lacks this ability. Sequence alignment experiments located the essential amino residues for the recognition of surface exposed phosphatidylserine within the calcium binding motifs common to all annexins. These amino acid residues were missing in the evolutionary young AnxA8 and when they were reintroduced by site directed mutagenesis AnxA8 gains the capability to interact with phosphatidylserine containing liposomes and apoptotic cells. By defining the evolutionary conserved amino acid residues mediating phosphatidylserine binding of annexins we show that the recognition of dying cells represent a common feature of most annexins. Hence, the individual annexin repertoire bound to the cell surface of dying cells may fulfil opsonin-like function in cell death recognition.Discrimination of viable from dying cells is a prerequisite for the efficient clearance of dying and dead cells and to suppress uncontrolled cell lysis and the release of potentially harmful cellular compounds to the local environment. During development and under normal physiological conditions, cells are removed through the process of apoptosis and undergo a strictly defined series of morphological and biochemical changes, before being engulfed by professional phagocytes such as macrophages or even by neighboring cells. A signature of specific "eat me" signals are exposed at the cell surface of apoptotic cells, which enable direct or indirect interactions with phagocytes and dying cells to promote the efficient clearance of apoptotic cells. This reduces the risk of accumulation of secondarily necrotic cells and the release of cellular content to the microenvironment. Exposure of apoptotic-cell associated molecular patterns together with recognition and interpretation of these by phagocytes are crucial steps in the appropriate response of phagocytes toward the engulfed cells (1).A hallmark of early apoptotic cells is the loss of membrane asymmetry and the exposure of anionic phosphatidylserine (PS) 3 on the outer lipid layer of the cells. In most cells PS predominantly resides in the inner leaflet of the plasma membrane, regulating membrane charge and protein localization (2). This membrane asymmetry is actively maintained by an inward transporting aminophospholipid translocase (3). Upon induction of apotosis, rising cytoplasmic Ca 2ϩ levels cause a loss of translocase activity and an activ...

show abstract

Evolutionary perspective on annexin calcium-binding domains

Cited by 74 publications

References 28 publications

History of biological metal utilization inferred through phylogenomic analysis of protein structures

History of biological metal utilization inferred through phylogenomic analysis of protein structures

Characterization of a Secretory Annexin in Echinococcus granulosus

Identification of Novel Binding Partners (Annexins) for the Cell Death Signal Phosphatidylserine and Definition of Their Recognition Motif

Contact Info

Product

Resources

About