title: The ADP-ribosyl cyclases--the current evolutionary state of the ARCs.
abstract: The major ADP-ribosylating enzyme families are the focus of this special issue of Frontiers in Bioscience . However, there is room for another family of enzymes with the capacity to utilize nicotinamide adenine dinucleotide (NAD): the ADP-ribosyl cyclases (ARCs). These unique enzymes catalyse the cyclization of NAD to cyclic ADP ribose (cADPR), a widely distributed second messenger. However, the ARCs are versatile enzymes that can manipulate NAD, NAD phosphate (NADP) and other substrates to generate various bioactive molecules including nicotinic acid adenine dinucleotide diphosphate (NAADP) and ADP ribose (ADPR). This review will focus on the group of well-characterized invertebrate and vertebrate ARCs whose common gene structure allows us to trace their origin to the ancestor of bilaterian animals. Behind a facade of gene and protein homology lies a family with a disparate functional repertoire dictated by the animal model and the physical trait under investigation. Here we present a phylogenetic view of the ARCs to better understand the evolution of function in this family.
authors.affiliation: Immunogenetics Lab, Department of Medical Sciences, University of Torino, Via Santena 19, 10126 Torino, Italy.
authors.forename: Enza
authors.initials: E
authors.lastname: Ferrero
authors.affiliation: Immunogenetics Lab, Department of Medical Sciences, University of Torino, Via Santena 19, 10126 Torino, Italy.
authors.forename: Nicola
authors.initials: N
authors.lastname: Lo Buono
authors.affiliation: Immunogenetics Lab, Department of Medical Sciences, University of Torino, Via Santena 19, 10126 Torino, Italy.
authors.forename: Alberto L
authors.initials: AL
authors.lastname: Horenstein
authors.affiliation: Immunogenetics Lab, Department of Medical Sciences, University of Torino, Via Santena 19, 10126 Torino, Italy.
authors.forename: Ada
authors.initials: A
authors.lastname: Funaro
authors.affiliation: Immunogenetics Lab, Department of Medical Sciences, University of Torino, Via Santena 19, 10126 Torino, Italy.
authors.forename: Fabio
authors.initials: F
authors.lastname: Malavasi
mesh_terms: D036541:ADP-ribosyl Cyclase / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D051997:ADP-ribosyl Cyclase 1 / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D015703:Antigens, CD / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D019143:Evolution, Molecular; D058851:GPI-Linked Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism; D006801:Humans; D009243:NAD / Q000378:metabolism; D010802:Phylogeny; D013045:Species Specificity
chemical_list: D015703:Antigens, CD; D058851:GPI-Linked Proteins; D009243:NAD; D036541:ADP-ribosyl Cyclase; C087521:ADP-ribosyl cyclase 2; D051997:ADP-ribosyl Cyclase 1