title: Ion channels, phosphorylation and mammalian sperm capacitation.
abstract: Sexually reproducing animals require an orchestrated communication between spermatozoa and the egg to generate a new individual. Capacitation, a maturational complex phenomenon that occurs in the female reproductive tract, renders spermatozoa capable of binding and fusing with the oocyte, and it is a requirement for mammalian fertilization. Capacitation encompasses plasma membrane reorganization, ion permeability regulation, cholesterol loss and changes in the phosphorylation state of many proteins. Novel tools to study sperm ion channels, image intracellular ionic changes and proteins with better spatial and temporal resolution, are unraveling how modifications in sperm ion transport and phosphorylation states lead to capacitation. Recent evidence indicates that two parallel pathways regulate phosphorylation events leading to capacitation, one of them requiring activation of protein kinase A and the second one involving inactivation of ser/thr phosphatases. This review examines the involvement of ion transporters and phosphorylation signaling processes needed for spermatozoa to achieve capacitation. Understanding the molecular mechanisms leading to fertilization is central for societies to deal with rising male infertility rates, to develop safe male gamete-based contraceptives and to preserve biodiversity through better assisted fertilization strategies.
authors.affiliation: Department of Veterinary and Animal Science, Paige Labs, University of Massachusets, Amherst, MA 01003, USA.
authors.forename: Pablo E
authors.initials: PE
authors.lastname: Visconti
authors.forename: Dario
authors.initials: D
authors.lastname: Krapf
authors.forename: José Luis
authors.initials: JL
authors.lastname: de la Vega-Beltrán
authors.forename: Juan José
authors.initials: JJ
authors.lastname: Acevedo
authors.forename: Alberto
authors.initials: A
authors.lastname: Darszon
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism; D015220:Calcium Channels; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000502:physiology; D053503:Epithelial Sodium Channels / Q000502:physiology; D005260:Female; D005306:Fertilization; D006863:Hydrogen-Ion Concentration; D007473:Ion Channels / Q000502:physiology*; D008297:Male; D021962:Membrane Microdomains / Q000502:physiology; D049294:Phospholipid Transfer Proteins / Q000502:physiology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation; D024661:Potassium Channels, Inwardly Rectifying / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D013075:Sperm Capacitation / Q000502:physiology*; D013094:Spermatozoa / Q000502:physiology; D019061:src-Family Kinases / Q000502:physiology
chemical_list: D015220:Calcium Channels; C488642:Catsper1 protein, mouse; D053503:Epithelial Sodium Channels; D007473:Ion Channels; D049294:Phospholipid Transfer Proteins; D024661:Potassium Channels, Inwardly Rectifying; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D019061:src-Family Kinases; D017868:Cyclic AMP-Dependent Protein Kinases; D010749:Phosphoprotein Phosphatases; D002118:Calcium