The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm

Autores
Alvau, Antonio; Battistone, Maria Agustina; Gervasi, Maria Gracia; Navarrete, Felipe A.; Xu, Xinran; Sánchez Cárdenas, Claudia; De la Vega Beltran, José Luis; Da Ros, Vanina Gabriela; Greer, Peter; Darszon, Alberto; Krapf, Diego; Salicioni, Ana María; Cuasnicu, Patricia Sara; Visconti, Pablo E.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Sperm capacitation is required for fertilization. At the molecular level, this process is associated with fast activation of protein kinase A. Downstream of this event, capacitating conditions lead to an increase in tyrosine phosphorylation. The identity of the tyrosine kinase(s) mediating this process has not been conclusively demonstrated. Recent experiments using stallion and human sperm have suggested a role for PYK2 based on the use of small molecule inhibitors directed against this kinase. However, crucially, loss-of-function experiments have not been reported. Here, we used both pharmacological inhibitors and genetically modified mice models to investigate the identity of the tyrosine kinase(s) mediating the increase in tyrosine phosphorylation in mouse sperm. Similar to stallion and human, PF431396 blocks the capacitation-associated increase in tyrosine phosphorylation. Yet, sperm from Pyk2(-/-) mice displayed a normal increase in tyrosine phosphorylation, implying that PYK2 is not responsible for this phosphorylation process. Here, we show that PF431396 can also inhibit FER, a tyrosine kinase known to be present in sperm. Sperm from mice targeted with a kinase-inactivating mutation in Fer failed to undergo capacitation-associated increases in tyrosine phosphorylation. Although these mice are fertile, their sperm displayed a reduced ability to fertilize metaphase II-arrested eggs in vitro.
Fil: Alvau, Antonio. University of Massachussets; Estados Unidos
Fil: Battistone, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Gervasi, Maria Gracia. University of Massachussets; Estados Unidos
Fil: Navarrete, Felipe A.. University of Massachussets; Estados Unidos
Fil: Xu, Xinran. State University of Colorado - Fort Collins; Estados Unidos
Fil: Sánchez Cárdenas, Claudia. Universidad Nacional Autónoma de México. Instituto de Biotecnología; México
Fil: De la Vega Beltran, José Luis. Universidad Nacional Autónoma de México. Instituto de Biotecnología; México
Fil: Da Ros, Vanina Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Greer, Peter. Queens University; Canadá
Fil: Darszon, Alberto. Universidad Nacional Autónoma de México. Instituto de Biotecnología; México
Fil: Krapf, Diego. State University of Colorado - Fort Collins; Estados Unidos
Fil: Salicioni, Ana María. University of Massachussets; Estados Unidos
Fil: Cuasnicu, Patricia Sara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Visconti, Pablo E.. University of Massachussets; Estados Unidos
Materia
FER
SPERM CAPACITATION
TYROSINE PHOSPHORYLATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/24029
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/24029
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine spermAlvau, AntonioBattistone, Maria AgustinaGervasi, Maria GraciaNavarrete, Felipe A.Xu, XinranSánchez Cárdenas, ClaudiaDe la Vega Beltran, José LuisDa Ros, Vanina GabrielaGreer, PeterDarszon, AlbertoKrapf, DiegoSalicioni, Ana MaríaCuasnicu, Patricia SaraVisconti, Pablo E.FERSPERM CAPACITATIONTYROSINE PHOSPHORYLATIONhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Sperm capacitation is required for fertilization. At the molecular level, this process is associated with fast activation of protein kinase A. Downstream of this event, capacitating conditions lead to an increase in tyrosine phosphorylation. The identity of the tyrosine kinase(s) mediating this process has not been conclusively demonstrated. Recent experiments using stallion and human sperm have suggested a role for PYK2 based on the use of small molecule inhibitors directed against this kinase. However, crucially, loss-of-function experiments have not been reported. Here, we used both pharmacological inhibitors and genetically modified mice models to investigate the identity of the tyrosine kinase(s) mediating the increase in tyrosine phosphorylation in mouse sperm. Similar to stallion and human, PF431396 blocks the capacitation-associated increase in tyrosine phosphorylation. Yet, sperm from Pyk2(-/-) mice displayed a normal increase in tyrosine phosphorylation, implying that PYK2 is not responsible for this phosphorylation process. Here, we show that PF431396 can also inhibit FER, a tyrosine kinase known to be present in sperm. Sperm from mice targeted with a kinase-inactivating mutation in Fer failed to undergo capacitation-associated increases in tyrosine phosphorylation. Although these mice are fertile, their sperm displayed a reduced ability to fertilize metaphase II-arrested eggs in vitro.Fil: Alvau, Antonio. University of Massachussets; Estados UnidosFil: Battistone, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Gervasi, Maria Gracia. University of Massachussets; Estados UnidosFil: Navarrete, Felipe A.. University of Massachussets; Estados UnidosFil: Xu, Xinran. State University of Colorado - Fort Collins; Estados UnidosFil: Sánchez Cárdenas, Claudia. Universidad Nacional Autónoma de México. Instituto de Biotecnología; MéxicoFil: De la Vega Beltran, José Luis. Universidad Nacional Autónoma de México. Instituto de Biotecnología; MéxicoFil: Da Ros, Vanina Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Greer, Peter. Queens University; CanadáFil: Darszon, Alberto. Universidad Nacional Autónoma de México. Instituto de Biotecnología; MéxicoFil: Krapf, Diego. State University of Colorado - Fort Collins; Estados UnidosFil: Salicioni, Ana María. University of Massachussets; Estados UnidosFil: Cuasnicu, Patricia Sara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Visconti, Pablo E.. University of Massachussets; Estados UnidosCompany of Biologists2016-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24029Alvau, Antonio; Battistone, Maria Agustina; Gervasi, Maria Gracia; Navarrete, Felipe A.; Xu, Xinran; et al.; The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm; Company of Biologists; Development; 143; 13; 7-2016; 2325-23330950-19911477-9129CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://dev.biologists.org/content/143/13/2325info:eu-repo/semantics/altIdentifier/doi/10.1242/dev.136499info:eu-repo/semantics/altIdentifier/pmid/27226326info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:48:31Zoai:ri.conicet.gov.ar:11336/24029instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:48:32.151CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
title The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
spellingShingle The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
Alvau, Antonio
FER
SPERM CAPACITATION
TYROSINE PHOSPHORYLATION
title_short The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
title_full The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
title_fullStr The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
title_full_unstemmed The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
title_sort The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm
dc.creator.none.fl_str_mv Alvau, Antonio
Battistone, Maria Agustina
Gervasi, Maria Gracia
Navarrete, Felipe A.
Xu, Xinran
Sánchez Cárdenas, Claudia
De la Vega Beltran, José Luis
Da Ros, Vanina Gabriela
Greer, Peter
Darszon, Alberto
Krapf, Diego
Salicioni, Ana María
Cuasnicu, Patricia Sara
Visconti, Pablo E.
author Alvau, Antonio
author_facet Alvau, Antonio
Battistone, Maria Agustina
Gervasi, Maria Gracia
Navarrete, Felipe A.
Xu, Xinran
Sánchez Cárdenas, Claudia
De la Vega Beltran, José Luis
Da Ros, Vanina Gabriela
Greer, Peter
Darszon, Alberto
Krapf, Diego
Salicioni, Ana María
Cuasnicu, Patricia Sara
Visconti, Pablo E.
author_role author
author2 Battistone, Maria Agustina
Gervasi, Maria Gracia
Navarrete, Felipe A.
Xu, Xinran
Sánchez Cárdenas, Claudia
De la Vega Beltran, José Luis
Da Ros, Vanina Gabriela
Greer, Peter
Darszon, Alberto
Krapf, Diego
Salicioni, Ana María
Cuasnicu, Patricia Sara
Visconti, Pablo E.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv FER
SPERM CAPACITATION
TYROSINE PHOSPHORYLATION
topic FER
SPERM CAPACITATION
TYROSINE PHOSPHORYLATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Sperm capacitation is required for fertilization. At the molecular level, this process is associated with fast activation of protein kinase A. Downstream of this event, capacitating conditions lead to an increase in tyrosine phosphorylation. The identity of the tyrosine kinase(s) mediating this process has not been conclusively demonstrated. Recent experiments using stallion and human sperm have suggested a role for PYK2 based on the use of small molecule inhibitors directed against this kinase. However, crucially, loss-of-function experiments have not been reported. Here, we used both pharmacological inhibitors and genetically modified mice models to investigate the identity of the tyrosine kinase(s) mediating the increase in tyrosine phosphorylation in mouse sperm. Similar to stallion and human, PF431396 blocks the capacitation-associated increase in tyrosine phosphorylation. Yet, sperm from Pyk2(-/-) mice displayed a normal increase in tyrosine phosphorylation, implying that PYK2 is not responsible for this phosphorylation process. Here, we show that PF431396 can also inhibit FER, a tyrosine kinase known to be present in sperm. Sperm from mice targeted with a kinase-inactivating mutation in Fer failed to undergo capacitation-associated increases in tyrosine phosphorylation. Although these mice are fertile, their sperm displayed a reduced ability to fertilize metaphase II-arrested eggs in vitro.
Fil: Alvau, Antonio. University of Massachussets; Estados Unidos
Fil: Battistone, Maria Agustina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Gervasi, Maria Gracia. University of Massachussets; Estados Unidos
Fil: Navarrete, Felipe A.. University of Massachussets; Estados Unidos
Fil: Xu, Xinran. State University of Colorado - Fort Collins; Estados Unidos
Fil: Sánchez Cárdenas, Claudia. Universidad Nacional Autónoma de México. Instituto de Biotecnología; México
Fil: De la Vega Beltran, José Luis. Universidad Nacional Autónoma de México. Instituto de Biotecnología; México
Fil: Da Ros, Vanina Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Greer, Peter. Queens University; Canadá
Fil: Darszon, Alberto. Universidad Nacional Autónoma de México. Instituto de Biotecnología; México
Fil: Krapf, Diego. State University of Colorado - Fort Collins; Estados Unidos
Fil: Salicioni, Ana María. University of Massachussets; Estados Unidos
Fil: Cuasnicu, Patricia Sara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Visconti, Pablo E.. University of Massachussets; Estados Unidos
description Sperm capacitation is required for fertilization. At the molecular level, this process is associated with fast activation of protein kinase A. Downstream of this event, capacitating conditions lead to an increase in tyrosine phosphorylation. The identity of the tyrosine kinase(s) mediating this process has not been conclusively demonstrated. Recent experiments using stallion and human sperm have suggested a role for PYK2 based on the use of small molecule inhibitors directed against this kinase. However, crucially, loss-of-function experiments have not been reported. Here, we used both pharmacological inhibitors and genetically modified mice models to investigate the identity of the tyrosine kinase(s) mediating the increase in tyrosine phosphorylation in mouse sperm. Similar to stallion and human, PF431396 blocks the capacitation-associated increase in tyrosine phosphorylation. Yet, sperm from Pyk2(-/-) mice displayed a normal increase in tyrosine phosphorylation, implying that PYK2 is not responsible for this phosphorylation process. Here, we show that PF431396 can also inhibit FER, a tyrosine kinase known to be present in sperm. Sperm from mice targeted with a kinase-inactivating mutation in Fer failed to undergo capacitation-associated increases in tyrosine phosphorylation. Although these mice are fertile, their sperm displayed a reduced ability to fertilize metaphase II-arrested eggs in vitro.
publishDate 2016
dc.date.none.fl_str_mv 2016-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/24029
Alvau, Antonio; Battistone, Maria Agustina; Gervasi, Maria Gracia; Navarrete, Felipe A.; Xu, Xinran; et al.; The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm; Company of Biologists; Development; 143; 13; 7-2016; 2325-2333
0950-1991
1477-9129
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24029
identifier_str_mv Alvau, Antonio; Battistone, Maria Agustina; Gervasi, Maria Gracia; Navarrete, Felipe A.; Xu, Xinran; et al.; The tyrosine kinase FER is responsible for the capacitation-associated increase in tyrosine phosphorylation in murine sperm; Company of Biologists; Development; 143; 13; 7-2016; 2325-2333
0950-1991
1477-9129
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://dev.biologists.org/content/143/13/2325
info:eu-repo/semantics/altIdentifier/doi/10.1242/dev.136499
info:eu-repo/semantics/altIdentifier/pmid/27226326
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Company of Biologists
publisher.none.fl_str_mv Company of Biologists
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.069144

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