Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin

Autores
Noguera, Martín Ezequiel; Primo, Maria Evangelina; Sosa, Laura Natalia Fidela; Risso, Valeria Alejandra; Poskus, Edgardo; Ermacora, Mario Roberto
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The receptor-type protein-tyrosine phosphatase (RPTP) phogrin is localized at the membrane of secretory granules of pancreatic islet ;-cells and, similarly to the closely related ICA512, plays a role in the regulation of insulin secretion, in ensuring proper granulogenesis and stability, and in the regulation of -cell growth. The mature membraneproximal ectodomain of phogrin (MPE phogrin) was produced as a recombinant protein and characterized. CD, fluorescence, controlled proteolysis, size-exclusion chromatography, and multi-angle light scattering showed that it is a properlyfolded monomeric domain. Equilibrium experiments, in the presence of guanidinium chloride and thermal unfolding, suggest a two-state mechanism with a G of 2.3-3.3 kcal/mol, respectively. The study establishes common features and differences of MPE phogrin and the homologous ectodomain of ICA512. A homology model of phogrin was built based in the x-ray structure of MPE ICA512. The model is a starting point for modeling the entire receptor and for testing the quaternary structure and interactions of this protein in vivo. A description of the membrane insertion mode and putative interacting surfaces of this large protein is fundamental for the understanding of its biological function.
Fil: Noguera, Martín Ezequiel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina
Fil: Primo, Maria Evangelina. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina. Consejo Nacional de Investigaciones Cienti­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "Profesor R. A. Margni"; Argentina
Fil: Sosa, Laura Natalia Fidela. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina. Consejo Nacional de Investigaciones Cienti­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "Profesor R. A. Margni"; Argentina
Fil: Risso, Valeria Alejandra. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina
Fil: Poskus, Edgardo. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina
Fil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina
Materia
Diabetes
Equilibrium Unfolding
Homology Modeling
Phogrin
Receptor-Type Protein-Tyrosine Phosphatase
Secretory Granule
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:11336/8032
Acceder
id CONICETDig_39db8911581bfd75f6171b75a8a811ee
oai_identifier_str oai:ri.conicet.gov.ar:11336/8032
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase PhogrinNoguera, Martín EzequielPrimo, Maria EvangelinaSosa, Laura Natalia FidelaRisso, Valeria AlejandraPoskus, EdgardoErmacora, Mario RobertoDiabetesEquilibrium UnfoldingHomology ModelingPhogrinReceptor-Type Protein-Tyrosine PhosphataseSecretory Granulehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The receptor-type protein-tyrosine phosphatase (RPTP) phogrin is localized at the membrane of secretory granules of pancreatic islet ;-cells and, similarly to the closely related ICA512, plays a role in the regulation of insulin secretion, in ensuring proper granulogenesis and stability, and in the regulation of -cell growth. The mature membraneproximal ectodomain of phogrin (MPE phogrin) was produced as a recombinant protein and characterized. CD, fluorescence, controlled proteolysis, size-exclusion chromatography, and multi-angle light scattering showed that it is a properlyfolded monomeric domain. Equilibrium experiments, in the presence of guanidinium chloride and thermal unfolding, suggest a two-state mechanism with a G of 2.3-3.3 kcal/mol, respectively. The study establishes common features and differences of MPE phogrin and the homologous ectodomain of ICA512. A homology model of phogrin was built based in the x-ray structure of MPE ICA512. The model is a starting point for modeling the entire receptor and for testing the quaternary structure and interactions of this protein in vivo. A description of the membrane insertion mode and putative interacting surfaces of this large protein is fundamental for the understanding of its biological function.Fil: Noguera, Martín Ezequiel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); ArgentinaFil: Primo, Maria Evangelina. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina. Consejo Nacional de Investigaciones Cienti­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "Profesor R. A. Margni"; ArgentinaFil: Sosa, Laura Natalia Fidela. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina. Consejo Nacional de Investigaciones Cienti­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "Profesor R. A. Margni"; ArgentinaFil: Risso, Valeria Alejandra. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); ArgentinaFil: Poskus, Edgardo. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; ArgentinaFil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); ArgentinaBentham Science Publishers2013-09info: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/11336/8032Noguera, Martín Ezequiel; Primo, Maria Evangelina; Sosa, Laura Natalia Fidela; Risso, Valeria Alejandra; Poskus, Edgardo; et al.; Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin; Bentham Science Publishers; Protein And Peptide Letters; 20; 9; 9-2013; 1009-10170929-8665enginfo:eu-repo/semantics/altIdentifier/doi/10.2174/0929866511320090007info:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/112939/articleinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:16:47Zoai:ri.conicet.gov.ar:11336/8032instacron: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 10:16:47.831CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
title Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
spellingShingle Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
Noguera, Martín Ezequiel
Diabetes
Equilibrium Unfolding
Homology Modeling
Phogrin
Receptor-Type Protein-Tyrosine Phosphatase
Secretory Granule
title_short Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
title_full Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
title_fullStr Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
title_full_unstemmed Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
title_sort Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin
dc.creator.none.fl_str_mv Noguera, Martín Ezequiel
Primo, Maria Evangelina
Sosa, Laura Natalia Fidela
Risso, Valeria Alejandra
Poskus, Edgardo
Ermacora, Mario Roberto
author Noguera, Martín Ezequiel
author_facet Noguera, Martín Ezequiel
Primo, Maria Evangelina
Sosa, Laura Natalia Fidela
Risso, Valeria Alejandra
Poskus, Edgardo
Ermacora, Mario Roberto
author_role author
author2 Primo, Maria Evangelina
Sosa, Laura Natalia Fidela
Risso, Valeria Alejandra
Poskus, Edgardo
Ermacora, Mario Roberto
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Diabetes
Equilibrium Unfolding
Homology Modeling
Phogrin
Receptor-Type Protein-Tyrosine Phosphatase
Secretory Granule
topic Diabetes
Equilibrium Unfolding
Homology Modeling
Phogrin
Receptor-Type Protein-Tyrosine Phosphatase
Secretory Granule
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The receptor-type protein-tyrosine phosphatase (RPTP) phogrin is localized at the membrane of secretory granules of pancreatic islet ;-cells and, similarly to the closely related ICA512, plays a role in the regulation of insulin secretion, in ensuring proper granulogenesis and stability, and in the regulation of -cell growth. The mature membraneproximal ectodomain of phogrin (MPE phogrin) was produced as a recombinant protein and characterized. CD, fluorescence, controlled proteolysis, size-exclusion chromatography, and multi-angle light scattering showed that it is a properlyfolded monomeric domain. Equilibrium experiments, in the presence of guanidinium chloride and thermal unfolding, suggest a two-state mechanism with a G of 2.3-3.3 kcal/mol, respectively. The study establishes common features and differences of MPE phogrin and the homologous ectodomain of ICA512. A homology model of phogrin was built based in the x-ray structure of MPE ICA512. The model is a starting point for modeling the entire receptor and for testing the quaternary structure and interactions of this protein in vivo. A description of the membrane insertion mode and putative interacting surfaces of this large protein is fundamental for the understanding of its biological function.
Fil: Noguera, Martín Ezequiel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina
Fil: Primo, Maria Evangelina. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina. Consejo Nacional de Investigaciones Cienti­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "Profesor R. A. Margni"; Argentina
Fil: Sosa, Laura Natalia Fidela. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina. Consejo Nacional de Investigaciones Cienti­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "Profesor R. A. Margni"; Argentina
Fil: Risso, Valeria Alejandra. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina
Fil: Poskus, Edgardo. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina. Universidad de Buenos Aires. Facultad de Medicina. Hospital de Clínicas General San Martín; Argentina
Fil: Ermacora, Mario Roberto. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto Multidisciplinario de Biología Celular (i); Argentina
description The receptor-type protein-tyrosine phosphatase (RPTP) phogrin is localized at the membrane of secretory granules of pancreatic islet ;-cells and, similarly to the closely related ICA512, plays a role in the regulation of insulin secretion, in ensuring proper granulogenesis and stability, and in the regulation of -cell growth. The mature membraneproximal ectodomain of phogrin (MPE phogrin) was produced as a recombinant protein and characterized. CD, fluorescence, controlled proteolysis, size-exclusion chromatography, and multi-angle light scattering showed that it is a properlyfolded monomeric domain. Equilibrium experiments, in the presence of guanidinium chloride and thermal unfolding, suggest a two-state mechanism with a G of 2.3-3.3 kcal/mol, respectively. The study establishes common features and differences of MPE phogrin and the homologous ectodomain of ICA512. A homology model of phogrin was built based in the x-ray structure of MPE ICA512. The model is a starting point for modeling the entire receptor and for testing the quaternary structure and interactions of this protein in vivo. A description of the membrane insertion mode and putative interacting surfaces of this large protein is fundamental for the understanding of its biological function.
publishDate 2013
dc.date.none.fl_str_mv 2013-09
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/11336/8032
Noguera, Martín Ezequiel; Primo, Maria Evangelina; Sosa, Laura Natalia Fidela; Risso, Valeria Alejandra; Poskus, Edgardo; et al.; Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin; Bentham Science Publishers; Protein And Peptide Letters; 20; 9; 9-2013; 1009-1017
0929-8665
url http://hdl.handle.net/11336/8032
identifier_str_mv Noguera, Martín Ezequiel; Primo, Maria Evangelina; Sosa, Laura Natalia Fidela; Risso, Valeria Alejandra; Poskus, Edgardo; et al.; Biophysical Characterization of the Membrane-proximal Ectodomain of the Receptor-type Protein-tyrosine Phosphatase Phogrin; Bentham Science Publishers; Protein And Peptide Letters; 20; 9; 9-2013; 1009-1017
0929-8665
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.2174/0929866511320090007
info:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/112939/article
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
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 13.070432

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