title: Acroplaxome, an F-actin-keratin-containing plate, anchors the acrosome to the nucleus during shaping of the spermatid head.
abstract: Nuclear shaping is a critical event during sperm development as demonstrated by the incidence of male infertility associated with abnormal sperm ad shaping. Herein, we demonstrate that mouse and rat spermatids assemble in the subacrosomal space a cytoskeletal scaffold containing F-actin and Sak57, a keratin ortholog. The cytoskeletal plate, designated acroplaxome, anchors the developing acrosome to the nuclear envelope. The acroplaxome consists of a marginal ring containing keratin 5 10-nm-thick filaments and F-actin. The ring is closely associated with the leading edge of the acrosome and to the nuclear envelope during the elongation of the spermatid head. Anchorage of the acroplaxome to the gradually shaping nucleus is not disrupted by hypotonic treatment and brief Triton X-100 extraction. By examining spermiogenesis in the azh mutant mouse, characterized by abnormal spermatid/sperm head shaping, we have determined that a deformity of the spermatid nucleus is restricted to the acroplaxome region. These findings lead to the suggestion that the acroplaxome nucleates an F-actin-keratin-containing assembly with the purpose of stabilizing and anchoring the developing acrosome during spermatid nuclear elongation. The acroplaxome may also provide a mechanical planar scaffold modulating external clutching forces generated by a stack of Sertoli cell F-actin-containing hoops encircling the elongating spermatid nucleus.
authors.affiliation: Department of Cell Biology and Anatomical Sciences, The Sophie Davis School of Biomedical Education/The City University of New York Medical School, New York New York 10031, USA. kier@med.cuny.edu
authors.forename: Abraham L
authors.initials: AL
authors.lastname: Kierszenbaum
authors.forename: Eugene
authors.initials: E
authors.lastname: Rivkin
authors.forename: Laura L
authors.initials: LL
authors.lastname: Tres
mesh_terms: D000177:Acrosome / Q000378:metabolism* / Q000648:ultrastructure; D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism* / Q000648:ultrastructure; D003001:Cloning, Molecular; D005455:Fluorescent Antibody Technique; D015723:Gene Library; D006801:Humans; D053569:Keratin-15; D053555:Keratin-5; D007633:Keratins / Q000378:metabolism*; D008297:Male; D051379:Mice; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D009685:Nuclear Envelope / Q000378:metabolism / Q000648:ultrastructure; D051381:Rats; D020539:Sequence Analysis, Protein; D012867:Skin / Q000166:cytology / Q000378:metabolism; D013087:Spermatids / Q000378:metabolism* / Q000648:ultrastructure; D013091:Spermatogenesis / Q000502:physiology; D013737:Testis / Q000166:cytology / Q000378:metabolism
chemical_list: D000199:Actins; C503940:KRT5 protein, human; D053569:Keratin-15; D053555:Keratin-5; C492053:Krt15 protein, mouse; C503939:Krt5 protein, rat; D007633:Keratins