Loss of partitioning-defective-3/isotype-specific interacting protein (par-3/ASIP) in the elongating spermatid of RA175 (IGSF4A/SynCAM)-deficient mice
Autor: | Eriko Fujita, Tomonori Hirose, Yuko Tanabe, Beat A. Imhof, Michel Aurrand-Lions, Tadashi Kasahara, Takashi Momoi, Shigeo Ohno |
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Jazyk: | angličtina |
Rok vydání: | 2007 |
Předmět: |
Male
endocrine system Cellular differentiation PDZ domain education Immunoglobulins Cell Cycle Proteins Biology ddc:616.07 Testis/chemistry/ cytology/metabolism Pathology and Forensic Medicine Asthenozoospermia/genetics Mice Testis Cell polarity medicine Protein Isoforms Animals Ternary complex Cell Differentiation/ genetics Immunoglobulins/analysis/genetics/metabolism/ physiology Adaptor Proteins Signal Transducing Genetics Mice Knockout Spermatid Cell adhesion molecule urogenital system Cell Adhesion Molecules/analysis/ deficiency/metabolism Tumor Suppressor Proteins fungi Cell Adhesion Molecule-1 Membrane Proteins Cell Differentiation Spermatid differentiation Spermatids humanities Cell biology medicine.anatomical_structure Membrane Proteins/analysis/genetics/metabolism/ physiology Asthenozoospermia Protein Isoforms/analysis/deficiency Immunoglobulin superfamily Tumor Suppressor Proteins/genetics/ physiology Cell Adhesion Molecules Spermatids/chemistry/ cytology/metabolism Regular Articles |
Zdroj: | American Journal of Pathology, Vol. 171, No 6 (2007) pp. 1800-1810 |
ISSN: | 0002-9440 |
Popis: | IGSF4a/RA175/SynCAM (RA175) and junctional adhesion molecules (Jams) are members of the immunoglobulin superfamily with a PDZ-binding domain at their C termini. Deficiency of Ra175 (Ra175(-/-)) as well as Jam-C deficiency (Jam-C(-/-)) causes the defect of the spermatid differentiation, oligo-astheno-teratozoospermia. Ra175(-/-) elongating spermatids fail to mature further, whereas Jam-C(-/-) round spermatids lose cell polarity, and most of Jam-C(-/-) elongated spermatids are completely lost. RA175 and Jam-C seem to have similar but distinct functional roles during spermatid differentiation. Here we show that the cell polarity protein Par-3 with PDZ domains, a binding partner of Jams, is one of the associated proteins of the cytoplasmic region of RA175 in testis. Par-3 and Jam-C are partly co-localized with RA175 in the elongating and elongated spermatids; their distributions overlapped with that of RA175 on the tips of the dorsal region of the head of the elongating spermatid (steps 9 to 12) in the wild type. In the Ra175(-/-) elongating spermatid, Par-3 was absent, and Jam-C was absent or abnormally localized. The RA175 formed a ternary complex with Jam-C via interaction with Par-3. The lack of the ternary complex in the Ra175(-/-) elongating spermatid may cause the defect of the specialized adhesion structures, resulting in the oligo-astheno-teratozoospermia. |
Databáze: | OpenAIRE |
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