X-ray structure of the mature ectodomain of phogrin

Autores
Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; Ermacora, Mario Roberto
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.
Fil: Noguera, Martín Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Primo, Maria Evangelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina
Fil: Jakoncic, Jean. Brookhaven National Laboratory; Estados Unidos
Fil: Poskus, Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina
Fil: Solimena, Michele. Technische Universität Dresden.; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
Materia
STRUCTURE
PHOGRIN
IA-2
DIMER
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:11336/102207

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network_name_str CONICET Digital (CONICET)
spelling X-ray structure of the mature ectodomain of phogrinNoguera, Martín EzequielPrimo, Maria EvangelinaJakoncic, JeanPoskus, EdgardoSolimena, MicheleErmacora, Mario RobertoSTRUCTUREPHOGRINIA-2DIMERhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.Fil: Noguera, Martín Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Primo, Maria Evangelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; ArgentinaFil: Jakoncic, Jean. Brookhaven National Laboratory; Estados UnidosFil: Poskus, Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; ArgentinaFil: Solimena, Michele. Technische Universität Dresden.; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; AlemaniaFil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaSpringer2015-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/102207Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; et al.; X-ray structure of the mature ectodomain of phogrin; Springer; Journal of Structural and Functional Genomics; 16; 1; 3-2015; 1-91345-711XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s10969-014-9191-0info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10969-014-9191-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:43:22Zoai:ri.conicet.gov.ar:11336/102207instacron: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 09:43:22.795CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv X-ray structure of the mature ectodomain of phogrin
title X-ray structure of the mature ectodomain of phogrin
spellingShingle X-ray structure of the mature ectodomain of phogrin
Noguera, Martín Ezequiel
STRUCTURE
PHOGRIN
IA-2
DIMER
title_short X-ray structure of the mature ectodomain of phogrin
title_full X-ray structure of the mature ectodomain of phogrin
title_fullStr X-ray structure of the mature ectodomain of phogrin
title_full_unstemmed X-ray structure of the mature ectodomain of phogrin
title_sort X-ray structure of the mature ectodomain of phogrin
dc.creator.none.fl_str_mv Noguera, Martín Ezequiel
Primo, Maria Evangelina
Jakoncic, Jean
Poskus, Edgardo
Solimena, Michele
Ermacora, Mario Roberto
author Noguera, Martín Ezequiel
author_facet Noguera, Martín Ezequiel
Primo, Maria Evangelina
Jakoncic, Jean
Poskus, Edgardo
Solimena, Michele
Ermacora, Mario Roberto
author_role author
author2 Primo, Maria Evangelina
Jakoncic, Jean
Poskus, Edgardo
Solimena, Michele
Ermacora, Mario Roberto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv STRUCTURE
PHOGRIN
IA-2
DIMER
topic STRUCTURE
PHOGRIN
IA-2
DIMER
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.
Fil: Noguera, Martín Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Primo, Maria Evangelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina
Fil: Jakoncic, Jean. Brookhaven National Laboratory; Estados Unidos
Fil: Poskus, Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina
Fil: Solimena, Michele. Technische Universität Dresden.; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina
description Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.
publishDate 2015
dc.date.none.fl_str_mv 2015-03
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/11336/102207
Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; et al.; X-ray structure of the mature ectodomain of phogrin; Springer; Journal of Structural and Functional Genomics; 16; 1; 3-2015; 1-9
1345-711X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/102207
identifier_str_mv Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; et al.; X-ray structure of the mature ectodomain of phogrin; Springer; Journal of Structural and Functional Genomics; 16; 1; 3-2015; 1-9
1345-711X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s10969-014-9191-0
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10969-014-9191-0
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
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dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
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dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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