Ring-like oligomers of synaptotagmins and related C2 domain proteins
- Autores
- Zanetti, Maria Natalia; Bello, Oscar Daniel; Wang, Jing; Coleman, Jeff; Cai, Yiying; Sindelar, Charles V.; Rothman, James E.; Krishnakumar, Shyam S.
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- We recently reported that the C2AB portion of Synaptotagmin 1 (Syt1) could selfassemble into Ca2+-sensitive ring-like oligomers on membranes, which could potentially regulate neurotransmitter release. Here we report that analogous ring-like oligomers assemble from the C2AB domains of other Syt isoforms (Syt2, Syt7, Syt9) as well as related C2 domain containing protein, Doc2B and extended Synaptotagmins (E-Syts). Evidently, circular oligomerization is a general and conserved structural aspect of many C2 domain proteins, including Synaptotagmins. Further, using electron microscopy combined with targeted mutations, we show that under physiologically relevant conditions, both the Syt1 ring assembly and its rapid disruption by Ca2+ involve the well-established functional surfaces on the C2B domain that are important for synaptic transmission. Our data suggests that ring formation may be triggered at an early step in synaptic vesicle docking and positions Syt1 to synchronize neurotransmitter release to Ca2+ influx.
Fil: Zanetti, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Bello, Oscar Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina
Fil: Wang, Jing. University of Yale. School of Medicine; Estados Unidos
Fil: Coleman, Jeff. University of Yale. School of Medicine; Estados Unidos
Fil: Cai, Yiying. University of Yale. School of Medicine; Estados Unidos
Fil: Sindelar, Charles V.. University of Yale. School of Medicine; Estados Unidos
Fil: Rothman, James E.. University of Yale. School of Medicine; Estados Unidos
Fil: Krishnakumar, Shyam S.. University of Yale. School of Medicine; Estados Unidos - Materia
-
Biophisics
Neuroscience
Membrane fusion
Estructural biology - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/183138
Ver los metadatos del registro completo
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Ring-like oligomers of synaptotagmins and related C2 domain proteinsZanetti, Maria NataliaBello, Oscar DanielWang, JingColeman, JeffCai, YiyingSindelar, Charles V.Rothman, James E.Krishnakumar, Shyam S.BiophisicsNeuroscienceMembrane fusionEstructural biologyhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We recently reported that the C2AB portion of Synaptotagmin 1 (Syt1) could selfassemble into Ca2+-sensitive ring-like oligomers on membranes, which could potentially regulate neurotransmitter release. Here we report that analogous ring-like oligomers assemble from the C2AB domains of other Syt isoforms (Syt2, Syt7, Syt9) as well as related C2 domain containing protein, Doc2B and extended Synaptotagmins (E-Syts). Evidently, circular oligomerization is a general and conserved structural aspect of many C2 domain proteins, including Synaptotagmins. Further, using electron microscopy combined with targeted mutations, we show that under physiologically relevant conditions, both the Syt1 ring assembly and its rapid disruption by Ca2+ involve the well-established functional surfaces on the C2B domain that are important for synaptic transmission. Our data suggests that ring formation may be triggered at an early step in synaptic vesicle docking and positions Syt1 to synchronize neurotransmitter release to Ca2+ influx.Fil: Zanetti, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Bello, Oscar Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; ArgentinaFil: Wang, Jing. University of Yale. School of Medicine; Estados UnidosFil: Coleman, Jeff. University of Yale. School of Medicine; Estados UnidosFil: Cai, Yiying. University of Yale. School of Medicine; Estados UnidosFil: Sindelar, Charles V.. University of Yale. School of Medicine; Estados UnidosFil: Rothman, James E.. University of Yale. School of Medicine; Estados UnidosFil: Krishnakumar, Shyam S.. University of Yale. School of Medicine; Estados UnidoseLife Sciences Publications2016-07info: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/11336/183138Zanetti, Maria Natalia; Bello, Oscar Daniel; Wang, Jing; Coleman, Jeff; Cai, Yiying; et al.; Ring-like oligomers of synaptotagmins and related C2 domain proteins; eLife Sciences Publications; eLife; 5; 7-2016; 1-152050-084XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/17262info:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.17262info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:39:18Zoai:ri.conicet.gov.ar:11336/183138instacron: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 09:39:19.184CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
title |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
spellingShingle |
Ring-like oligomers of synaptotagmins and related C2 domain proteins Zanetti, Maria Natalia Biophisics Neuroscience Membrane fusion Estructural biology |
title_short |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
title_full |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
title_fullStr |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
title_full_unstemmed |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
title_sort |
Ring-like oligomers of synaptotagmins and related C2 domain proteins |
dc.creator.none.fl_str_mv |
Zanetti, Maria Natalia Bello, Oscar Daniel Wang, Jing Coleman, Jeff Cai, Yiying Sindelar, Charles V. Rothman, James E. Krishnakumar, Shyam S. |
author |
Zanetti, Maria Natalia |
author_facet |
Zanetti, Maria Natalia Bello, Oscar Daniel Wang, Jing Coleman, Jeff Cai, Yiying Sindelar, Charles V. Rothman, James E. Krishnakumar, Shyam S. |
author_role |
author |
author2 |
Bello, Oscar Daniel Wang, Jing Coleman, Jeff Cai, Yiying Sindelar, Charles V. Rothman, James E. Krishnakumar, Shyam S. |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Biophisics Neuroscience Membrane fusion Estructural biology |
topic |
Biophisics Neuroscience Membrane fusion Estructural biology |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
We recently reported that the C2AB portion of Synaptotagmin 1 (Syt1) could selfassemble into Ca2+-sensitive ring-like oligomers on membranes, which could potentially regulate neurotransmitter release. Here we report that analogous ring-like oligomers assemble from the C2AB domains of other Syt isoforms (Syt2, Syt7, Syt9) as well as related C2 domain containing protein, Doc2B and extended Synaptotagmins (E-Syts). Evidently, circular oligomerization is a general and conserved structural aspect of many C2 domain proteins, including Synaptotagmins. Further, using electron microscopy combined with targeted mutations, we show that under physiologically relevant conditions, both the Syt1 ring assembly and its rapid disruption by Ca2+ involve the well-established functional surfaces on the C2B domain that are important for synaptic transmission. Our data suggests that ring formation may be triggered at an early step in synaptic vesicle docking and positions Syt1 to synchronize neurotransmitter release to Ca2+ influx. Fil: Zanetti, Maria Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina Fil: Bello, Oscar Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina Fil: Wang, Jing. University of Yale. School of Medicine; Estados Unidos Fil: Coleman, Jeff. University of Yale. School of Medicine; Estados Unidos Fil: Cai, Yiying. University of Yale. School of Medicine; Estados Unidos Fil: Sindelar, Charles V.. University of Yale. School of Medicine; Estados Unidos Fil: Rothman, James E.. University of Yale. School of Medicine; Estados Unidos Fil: Krishnakumar, Shyam S.. University of Yale. School of Medicine; Estados Unidos |
description |
We recently reported that the C2AB portion of Synaptotagmin 1 (Syt1) could selfassemble into Ca2+-sensitive ring-like oligomers on membranes, which could potentially regulate neurotransmitter release. Here we report that analogous ring-like oligomers assemble from the C2AB domains of other Syt isoforms (Syt2, Syt7, Syt9) as well as related C2 domain containing protein, Doc2B and extended Synaptotagmins (E-Syts). Evidently, circular oligomerization is a general and conserved structural aspect of many C2 domain proteins, including Synaptotagmins. Further, using electron microscopy combined with targeted mutations, we show that under physiologically relevant conditions, both the Syt1 ring assembly and its rapid disruption by Ca2+ involve the well-established functional surfaces on the C2B domain that are important for synaptic transmission. Our data suggests that ring formation may be triggered at an early step in synaptic vesicle docking and positions Syt1 to synchronize neurotransmitter release to Ca2+ influx. |
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/11336/183138 Zanetti, Maria Natalia; Bello, Oscar Daniel; Wang, Jing; Coleman, Jeff; Cai, Yiying; et al.; Ring-like oligomers of synaptotagmins and related C2 domain proteins; eLife Sciences Publications; eLife; 5; 7-2016; 1-15 2050-084X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/183138 |
identifier_str_mv |
Zanetti, Maria Natalia; Bello, Oscar Daniel; Wang, Jing; Coleman, Jeff; Cai, Yiying; et al.; Ring-like oligomers of synaptotagmins and related C2 domain proteins; eLife Sciences Publications; eLife; 5; 7-2016; 1-15 2050-084X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://elifesciences.org/articles/17262 info:eu-repo/semantics/altIdentifier/doi/10.7554/eLife.17262 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
eLife Sciences Publications |
publisher.none.fl_str_mv |
eLife Sciences Publications |
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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1844613243676393472 |
score |
13.070432 |