title: GMAP210 and IFT88 are present in the spermatid golgi apparatus and participate in the development of the acrosome-acroplaxome complex, head-tail coupling apparatus and tail.
abstract: We describe the localization of the golgin GMAP210 and the intraflagellar protein IFT88 in the Golgi of spermatids and the participation of these two proteins in the development of the acrosome-acroplaxome complex, the head-tail coupling apparatus (HTCA) and the spermatid tail. Immunocytochemical experiments show that GMAP210 predominates in the cis-Golgi, whereas IFT88 prevails in the trans-Golgi network. Both proteins colocalize in proacrosomal vesicles, along acrosome membranes, the HTCA and the developing tail. IFT88 persists in the acrosome-acroplaxome region of the sperm head, whereas GMAP210 is no longer seen there. Spermatids of the Ift88 mouse mutant display abnormal head shaping and are tail-less. GMAP210 is visualized in the Ift88 mutant during acrosome-acroplaxome biogenesis. However, GMAP210-stained vesicles, mitochondria and outer dense fiber material build up in the manchette region and fail to reach the abortive tail stump in the mutant. In vitro disruption of the spermatid Golgi and microtubules with Brefeldin-A and nocodazole blocks the progression of GMAP210- and IFT88-stained proacrosomal vesicles to the acrosome-acroplaxome complex but F-actin distribution in the acroplaxome is not affected. We provide the first evidence that IFT88 is present in the Golgi of spermatids, that the microtubule-associated golgin GMAP210 and IFT88 participate in acrosome, HTCA, and tail biogenesis, and that defective intramanchette transport of cargos disrupts spermatid tail development.
authors.affiliation: Department of Cell Biology and Anatomy, The Sophie Davis School of Biomedical Education, The City University of New York, New York, New York, 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
authors.forename: Bradley K
authors.initials: BK
authors.lastname: Yoder
authors.forename: Courtney J
authors.initials: CJ
authors.lastname: Haycraft
authors.forename: Michel
authors.initials: M
authors.lastname: Bornens
authors.forename: Rosa M
authors.initials: RM
authors.lastname: Rios
mesh_terms: D000177:Acrosome / Q000378:metabolism* / Q000648:ultrastructure; D000199:Actins / Q000378:metabolism; D000818:Animals; D020126:Brefeldin A / Q000494:pharmacology; D003598:Cytoskeletal Proteins; D019084:Fluorescent Antibody Technique, Indirect; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D015151:Immunoblotting; D007150:Immunohistochemistry; D008297:Male; D051379:Mice; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism / Q000648:ultrastructure; D015739:Nocodazole / Q000494:pharmacology; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013087:Spermatids / Q000378:metabolism* / Q000648:ultrastructure; D025521:Tumor Suppressor Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D009687:Nuclear Proteins; C534613:TRIP11 protein, mouse; C490898:Tg737Rpw protein, mouse; D025521:Tumor Suppressor Proteins; D020126:Brefeldin A; D015739:Nocodazole