title: Biology and regulation of ectoplasmic specialization, an atypical adherens junction type, in the testis.
abstract: Anchoring junctions are cell adhesion apparatus present in all epithelia and endothelia. They are found at the cell-cell interface (adherens junction (AJ) and desmosome) and cell-matrix interface (focal contact and hemidesmosome). In this review, we focus our discussion on AJ in particular the dynamic changes and regulation of this junction type in normal epithelia using testis as a model. There are extensive restructuring of AJ (e.g., ectoplasmic specialization, ES, a testis-specific AJ) at the Sertoli-Sertoli cell interface (basal ES) and Sertoli-elongating spermatid interface (apical ES) during the seminiferous epithelial cycle of spermatogenesis to facilitate the migration of developing germ cells across the seminiferous epithelium. Furthermore, recent findings have shown that ES also confers cell orientation and polarity in the seminiferous epithelium, illustrating that some of the functions initially ascribed to tight junctions (TJ), such as conferring cell polarity, are also part of the inherent properties of the AJ (e.g., apical ES) in the testis. The biology and regulation based on recent studies in the testis are of interest to cell biologists in the field, in particular their regulation, which perhaps is applicable to tumorigenesis.
authors: Center for Biomedical Research, Population Council, 1230 York Avenue, New York, NY 10065, USA.
authors: Elissa W P
authors: EW
authors: Wong
authors: Dolores D
authors: DD
authors: Mruk
authors: C Yan
authors: CY
authors: Cheng
mesh_terms: D022005:Adherens Junctions / Q000502:physiology* / Q000648:ultrastructure*; D000818:Animals; D016764:Cell Polarity; D004705:Endocytosis; D006706:Homeostasis; D006801:Humans; D008297:Male; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology; D008954:Models, Biological; D046912:Multiprotein Complexes; D010447:Peptide Hydrolases / Q000502:physiology; D010749:Phosphoprotein Phosphatases / Q000502:physiology; D011480:Protease Inhibitors / Q000378:metabolism; D011494:Protein Kinases / Q000502:physiology; D012670:Seminiferous Epithelium / Q000502:physiology / Q000648:ultrastructure; D013091:Spermatogenesis; D013737:Testis / Q000502:physiology* / Q000648:ultrastructure*
chemical_list: D008565:Membrane Proteins; D046912:Multiprotein Complexes; D011480:Protease Inhibitors; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases; D010447:Peptide Hydrolases