Expression of full-length and truncated Fyn tyrosine kinase transcripts and encoded proteins during spermatogenesis and localization during acrosome biogenesis and fertilization
We report that full‐length and truncated transcripts of Fyn tyrosine protein kinase are expressed during testicular development. Truncated Fyn (tr‐Fyn) transcripts encode a 24 kDa protein with a N‐terminal (NT) domain, a complete Src homology (SH) 3 domain and an incomplete SH2 domain. The kinase do...
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| Veröffentlicht in: | Molecular reproduction and development 2009-09, Vol.76 (9), p.832-843 |
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| creator | Kierszenbaum, Abraham L. Rivkin, Eugene Talmor-Cohen, Anat Shalgi, Ruth Tres, Laura L. |
| description | We report that full‐length and truncated transcripts of Fyn tyrosine protein kinase are expressed during testicular development. Truncated Fyn (tr‐Fyn) transcripts encode a 24 kDa protein with a N‐terminal (NT) domain, a complete Src homology (SH) 3 domain and an incomplete SH2 domain. The kinase domain is missing in tr‐Fyn. In contrast, full‐length Fyn transcripts encode a 59–55 kDa protein. Fractionated spermatids by centrifugal elutriation express tr‐Fyn transcripts and protein, but not full‐length Fyn transcripts and protein. Neither full‐length Fyn nor tr‐Fyn transcripts and encoded proteins are detected in elutriated pachytene spermatocytes. Sertoli cells express full‐length and truncated Fyn throughout testicular development. In contrast, sperm contain full‐length Fyn transcripts and protein but not the truncated form. tr‐Fyn protein is visualized at the cytosolic side of Golgi membranes, derived proacrosomal vesicles, along the outer acrosome membrane and the inner acrosome membrane–acroplaxome complex anchoring the acrosome to the spermatid nuclear envelope. Fyn and phosphotyrosine immunoreactivity coexist in the tail of capacitated sperm. During fertilization, the Fyn‐containing acroplaxome seen in the egg‐bound and egg‐fused sperm is no longer detected upon decondensation of the sperm nucleus. tr‐Fyn expands the catalog of truncated tyrosine protein kinases expressed during spermiogenesis. We suggest that the NT and SH3 domains of tr‐Fyn may recruit adaptor and effector proteins, in particular GTPase activating proteins, required for acrosome–acroplaxome biogenesis, acroplaxome F‐actin dynamics and Sertoli cell function. During fertilization, full‐length Fyn in the acroplaxome may contribute to a transient local signaling burst during the early events of sperm–egg interaction. Mol. Reprod. Dev. 76: 832–843, 2009. © 2009 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/mrd.21049 |
| format | Article |
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Truncated Fyn (tr‐Fyn) transcripts encode a 24 kDa protein with a N‐terminal (NT) domain, a complete Src homology (SH) 3 domain and an incomplete SH2 domain. The kinase domain is missing in tr‐Fyn. In contrast, full‐length Fyn transcripts encode a 59–55 kDa protein. Fractionated spermatids by centrifugal elutriation express tr‐Fyn transcripts and protein, but not full‐length Fyn transcripts and protein. Neither full‐length Fyn nor tr‐Fyn transcripts and encoded proteins are detected in elutriated pachytene spermatocytes. Sertoli cells express full‐length and truncated Fyn throughout testicular development. In contrast, sperm contain full‐length Fyn transcripts and protein but not the truncated form. tr‐Fyn protein is visualized at the cytosolic side of Golgi membranes, derived proacrosomal vesicles, along the outer acrosome membrane and the inner acrosome membrane–acroplaxome complex anchoring the acrosome to the spermatid nuclear envelope. Fyn and phosphotyrosine immunoreactivity coexist in the tail of capacitated sperm. During fertilization, the Fyn‐containing acroplaxome seen in the egg‐bound and egg‐fused sperm is no longer detected upon decondensation of the sperm nucleus. tr‐Fyn expands the catalog of truncated tyrosine protein kinases expressed during spermiogenesis. We suggest that the NT and SH3 domains of tr‐Fyn may recruit adaptor and effector proteins, in particular GTPase activating proteins, required for acrosome–acroplaxome biogenesis, acroplaxome F‐actin dynamics and Sertoli cell function. During fertilization, full‐length Fyn in the acroplaxome may contribute to a transient local signaling burst during the early events of sperm–egg interaction. Mol. Reprod. Dev. 76: 832–843, 2009. © 2009 Wiley‐Liss, Inc.</description><identifier>ISSN: 1040-452X</identifier><identifier>EISSN: 1098-2795</identifier><identifier>DOI: 10.1002/mrd.21049</identifier><identifier>PMID: 19441121</identifier><identifier>CODEN: MREDEE</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Acrosome - metabolism ; Animals ; Biological and medical sciences ; Fertilization - physiology ; Fundamental and applied biological sciences. Psychology ; Immunohistochemistry ; Male ; Mammalian male genital system ; Microscopy, Electron ; Microscopy, Fluorescence ; Morphology. Physiology ; Proto-Oncogene Proteins c-fyn - biosynthesis ; Proto-Oncogene Proteins c-fyn - chemistry ; Proto-Oncogene Proteins c-fyn - genetics ; Rats ; Rats, Sprague-Dawley ; Reverse Transcriptase Polymerase Chain Reaction ; Sertoli Cells - metabolism ; Sperm Capacitation ; Spermatids - metabolism ; Spermatogenesis - physiology ; Spermatozoa - metabolism ; Testis - metabolism ; Vertebrates: reproduction</subject><ispartof>Molecular reproduction and development, 2009-09, Vol.76 (9), p.832-843</ispartof><rights>Copyright © 2009 Wiley‐Liss, Inc.</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4889-2e312e192b37efc4a26dacc9899198ee4a08a8c9834a8bbe9e536c8e635c248d3</citedby><cites>FETCH-LOGICAL-c4889-2e312e192b37efc4a26dacc9899198ee4a08a8c9834a8bbe9e536c8e635c248d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fmrd.21049$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fmrd.21049$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21691197$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19441121$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kierszenbaum, Abraham L.</creatorcontrib><creatorcontrib>Rivkin, Eugene</creatorcontrib><creatorcontrib>Talmor-Cohen, Anat</creatorcontrib><creatorcontrib>Shalgi, Ruth</creatorcontrib><creatorcontrib>Tres, Laura L.</creatorcontrib><title>Expression of full-length and truncated Fyn tyrosine kinase transcripts and encoded proteins during spermatogenesis and localization during acrosome biogenesis and fertilization</title><title>Molecular reproduction and development</title><addtitle>Mol. Reprod. Dev</addtitle><description>We report that full‐length and truncated transcripts of Fyn tyrosine protein kinase are expressed during testicular development. Truncated Fyn (tr‐Fyn) transcripts encode a 24 kDa protein with a N‐terminal (NT) domain, a complete Src homology (SH) 3 domain and an incomplete SH2 domain. The kinase domain is missing in tr‐Fyn. In contrast, full‐length Fyn transcripts encode a 59–55 kDa protein. Fractionated spermatids by centrifugal elutriation express tr‐Fyn transcripts and protein, but not full‐length Fyn transcripts and protein. Neither full‐length Fyn nor tr‐Fyn transcripts and encoded proteins are detected in elutriated pachytene spermatocytes. Sertoli cells express full‐length and truncated Fyn throughout testicular development. In contrast, sperm contain full‐length Fyn transcripts and protein but not the truncated form. tr‐Fyn protein is visualized at the cytosolic side of Golgi membranes, derived proacrosomal vesicles, along the outer acrosome membrane and the inner acrosome membrane–acroplaxome complex anchoring the acrosome to the spermatid nuclear envelope. Fyn and phosphotyrosine immunoreactivity coexist in the tail of capacitated sperm. During fertilization, the Fyn‐containing acroplaxome seen in the egg‐bound and egg‐fused sperm is no longer detected upon decondensation of the sperm nucleus. tr‐Fyn expands the catalog of truncated tyrosine protein kinases expressed during spermiogenesis. We suggest that the NT and SH3 domains of tr‐Fyn may recruit adaptor and effector proteins, in particular GTPase activating proteins, required for acrosome–acroplaxome biogenesis, acroplaxome F‐actin dynamics and Sertoli cell function. 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Physiology</subject><subject>Proto-Oncogene Proteins c-fyn - biosynthesis</subject><subject>Proto-Oncogene Proteins c-fyn - chemistry</subject><subject>Proto-Oncogene Proteins c-fyn - genetics</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sertoli Cells - metabolism</subject><subject>Sperm Capacitation</subject><subject>Spermatids - metabolism</subject><subject>Spermatogenesis - physiology</subject><subject>Spermatozoa - metabolism</subject><subject>Testis - metabolism</subject><subject>Vertebrates: reproduction</subject><issn>1040-452X</issn><issn>1098-2795</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0d9v1SAUB_DGaNycPvgPGF408aEbUNrCo5m70-TOGX9kvhFKT6-4Fjqgcdf_yv9Q7trN-LD4BIQP5-TwzbLnBB8SjOnR4NtDSjATD7J9ggXPaS3Kh7s9wzkr6be97EkIPzDGQnD8ONsjgjFCKNnPfp9cjx5CMM4i16Fu6vu8B7uJ35GyLYp-slpFaNFqa1HceheMBXRprAqQbpUN2psxhhsNVrs22dG7CMYG1E7e2A0KI_hBRbcBC8HMtnda9eaXirvOi1M61XcDoMb8Yzvw0dzip9mjTvUBni3rQfZ1dfLl-F2-Pj99f_xmnWvGucgpFIQCEbQpaug0U7RqldaCC0EEB2AKc8XTuWCKNw0IKItKc6iKUlPG2-IgezXXTdNcTRCiHEzQ0PfKgpuCrGom0qeT_0KKK0Yo5Qm-nuFuzOChk6M3g_JbSbDcBSlTkPImyGRfLEWnZoD2r1ySS-DlAlRIP9mlKLQJd46SShAi6uSOZvfT9LC9v6M8-_T2tnU-vzAhwvXdC-Uv08xFXcqLD6fyYl1_Fh9XZ5IVfwCz2cmF</recordid><startdate>200909</startdate><enddate>200909</enddate><creator>Kierszenbaum, Abraham L.</creator><creator>Rivkin, Eugene</creator><creator>Talmor-Cohen, Anat</creator><creator>Shalgi, Ruth</creator><creator>Tres, Laura L.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>200909</creationdate><title>Expression of full-length and truncated Fyn tyrosine kinase transcripts and encoded proteins during spermatogenesis and localization during acrosome biogenesis and fertilization</title><author>Kierszenbaum, Abraham L. ; Rivkin, Eugene ; Talmor-Cohen, Anat ; Shalgi, Ruth ; Tres, Laura L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4889-2e312e192b37efc4a26dacc9899198ee4a08a8c9834a8bbe9e536c8e635c248d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Acrosome - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Fertilization - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunohistochemistry</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Microscopy, Electron</topic><topic>Microscopy, Fluorescence</topic><topic>Morphology. Physiology</topic><topic>Proto-Oncogene Proteins c-fyn - biosynthesis</topic><topic>Proto-Oncogene Proteins c-fyn - chemistry</topic><topic>Proto-Oncogene Proteins c-fyn - genetics</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sertoli Cells - metabolism</topic><topic>Sperm Capacitation</topic><topic>Spermatids - metabolism</topic><topic>Spermatogenesis - physiology</topic><topic>Spermatozoa - metabolism</topic><topic>Testis - metabolism</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kierszenbaum, Abraham L.</creatorcontrib><creatorcontrib>Rivkin, Eugene</creatorcontrib><creatorcontrib>Talmor-Cohen, Anat</creatorcontrib><creatorcontrib>Shalgi, Ruth</creatorcontrib><creatorcontrib>Tres, Laura L.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular reproduction and development</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kierszenbaum, Abraham L.</au><au>Rivkin, Eugene</au><au>Talmor-Cohen, Anat</au><au>Shalgi, Ruth</au><au>Tres, Laura L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression of full-length and truncated Fyn tyrosine kinase transcripts and encoded proteins during spermatogenesis and localization during acrosome biogenesis and fertilization</atitle><jtitle>Molecular reproduction and development</jtitle><addtitle>Mol. Reprod. Dev</addtitle><date>2009-09</date><risdate>2009</risdate><volume>76</volume><issue>9</issue><spage>832</spage><epage>843</epage><pages>832-843</pages><issn>1040-452X</issn><eissn>1098-2795</eissn><coden>MREDEE</coden><abstract>We report that full‐length and truncated transcripts of Fyn tyrosine protein kinase are expressed during testicular development. Truncated Fyn (tr‐Fyn) transcripts encode a 24 kDa protein with a N‐terminal (NT) domain, a complete Src homology (SH) 3 domain and an incomplete SH2 domain. The kinase domain is missing in tr‐Fyn. In contrast, full‐length Fyn transcripts encode a 59–55 kDa protein. Fractionated spermatids by centrifugal elutriation express tr‐Fyn transcripts and protein, but not full‐length Fyn transcripts and protein. Neither full‐length Fyn nor tr‐Fyn transcripts and encoded proteins are detected in elutriated pachytene spermatocytes. Sertoli cells express full‐length and truncated Fyn throughout testicular development. In contrast, sperm contain full‐length Fyn transcripts and protein but not the truncated form. tr‐Fyn protein is visualized at the cytosolic side of Golgi membranes, derived proacrosomal vesicles, along the outer acrosome membrane and the inner acrosome membrane–acroplaxome complex anchoring the acrosome to the spermatid nuclear envelope. Fyn and phosphotyrosine immunoreactivity coexist in the tail of capacitated sperm. During fertilization, the Fyn‐containing acroplaxome seen in the egg‐bound and egg‐fused sperm is no longer detected upon decondensation of the sperm nucleus. tr‐Fyn expands the catalog of truncated tyrosine protein kinases expressed during spermiogenesis. We suggest that the NT and SH3 domains of tr‐Fyn may recruit adaptor and effector proteins, in particular GTPase activating proteins, required for acrosome–acroplaxome biogenesis, acroplaxome F‐actin dynamics and Sertoli cell function. During fertilization, full‐length Fyn in the acroplaxome may contribute to a transient local signaling burst during the early events of sperm–egg interaction. Mol. Reprod. Dev. 76: 832–843, 2009. © 2009 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>19441121</pmid><doi>10.1002/mrd.21049</doi><tpages>12</tpages></addata></record> |
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| subjects | Acrosome - metabolism Animals Biological and medical sciences Fertilization - physiology Fundamental and applied biological sciences. Psychology Immunohistochemistry Male Mammalian male genital system Microscopy, Electron Microscopy, Fluorescence Morphology. Physiology Proto-Oncogene Proteins c-fyn - biosynthesis Proto-Oncogene Proteins c-fyn - chemistry Proto-Oncogene Proteins c-fyn - genetics Rats Rats, Sprague-Dawley Reverse Transcriptase Polymerase Chain Reaction Sertoli Cells - metabolism Sperm Capacitation Spermatids - metabolism Spermatogenesis - physiology Spermatozoa - metabolism Testis - metabolism Vertebrates: reproduction |
| title | Expression of full-length and truncated Fyn tyrosine kinase transcripts and encoded proteins during spermatogenesis and localization during acrosome biogenesis and fertilization |
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