Cargando…

Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation

G protein‐activated inward‐rectifying potassium (K(+)) channels (Kir3/GIRK) participate in cell excitability. The GIRK5 channel is present in Xenopus laevis oocytes. In an attempt to investigate the physiological role of GIRK5, we identified a noncanonical di‐arginine endoplasmic reticulum (ER) rete...

Descripción completa

Detalles Bibliográficos
Autores principales: Rangel‐Garcia, Claudia I., Salvador, Carolina, Chavez‐Garcia, Karla, Diaz‐Bello, Beatriz, Lopez‐Gonzalez, Zinaeli, Vazquez‐Cruz, Lourdes, Angel Vazquez‐Martinez, Julio, Ortiz‐Navarrete, Vianney, Riveros‐Rosas, Hector, Escobar, Laura I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8016131/
https://www.ncbi.nlm.nih.gov/pubmed/33565726
http://dx.doi.org/10.1002/2211-5463.13113
_version_ 1783673794679799808
author Rangel‐Garcia, Claudia I.
Salvador, Carolina
Chavez‐Garcia, Karla
Diaz‐Bello, Beatriz
Lopez‐Gonzalez, Zinaeli
Vazquez‐Cruz, Lourdes
Angel Vazquez‐Martinez, Julio
Ortiz‐Navarrete, Vianney
Riveros‐Rosas, Hector
Escobar, Laura I.
author_facet Rangel‐Garcia, Claudia I.
Salvador, Carolina
Chavez‐Garcia, Karla
Diaz‐Bello, Beatriz
Lopez‐Gonzalez, Zinaeli
Vazquez‐Cruz, Lourdes
Angel Vazquez‐Martinez, Julio
Ortiz‐Navarrete, Vianney
Riveros‐Rosas, Hector
Escobar, Laura I.
author_sort Rangel‐Garcia, Claudia I.
collection PubMed
description G protein‐activated inward‐rectifying potassium (K(+)) channels (Kir3/GIRK) participate in cell excitability. The GIRK5 channel is present in Xenopus laevis oocytes. In an attempt to investigate the physiological role of GIRK5, we identified a noncanonical di‐arginine endoplasmic reticulum (ER) retention motif (KRXY). This retention motif is located at the N‐terminal region of GIRK5, coded by two small exons found only in X. laevis and X. tropicalis. These novel exons are expressed through use of an alternative transcription start site. Mutations in the sequence KRXY produced functional channels and induced progesterone‐independent oocyte meiotic progression. The chimeric proteins enhanced green fluorescent protein (EGFP)‐GIRK5‐WT and the EGFP‐GIRK5K13AR14A double mutant, were localized to the ER and the plasma membrane of the vegetal pole of the oocyte, respectively. Silencing of GIRK5 or blocking of this channel by external barium prevented progesterone‐induced meiotic progression. The endogenous level of GIRK5 protein decreased through oocyte stages in prophase I augmenting by progesterone. In conclusion, we have identified a unique mechanism by which the expression pattern of a K(+) channel evolved to control Xenopus oocyte maturation.
format Online
Article
Text
id pubmed-8016131
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-80161312021-04-02 Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation Rangel‐Garcia, Claudia I. Salvador, Carolina Chavez‐Garcia, Karla Diaz‐Bello, Beatriz Lopez‐Gonzalez, Zinaeli Vazquez‐Cruz, Lourdes Angel Vazquez‐Martinez, Julio Ortiz‐Navarrete, Vianney Riveros‐Rosas, Hector Escobar, Laura I. FEBS Open Bio Research Articles G protein‐activated inward‐rectifying potassium (K(+)) channels (Kir3/GIRK) participate in cell excitability. The GIRK5 channel is present in Xenopus laevis oocytes. In an attempt to investigate the physiological role of GIRK5, we identified a noncanonical di‐arginine endoplasmic reticulum (ER) retention motif (KRXY). This retention motif is located at the N‐terminal region of GIRK5, coded by two small exons found only in X. laevis and X. tropicalis. These novel exons are expressed through use of an alternative transcription start site. Mutations in the sequence KRXY produced functional channels and induced progesterone‐independent oocyte meiotic progression. The chimeric proteins enhanced green fluorescent protein (EGFP)‐GIRK5‐WT and the EGFP‐GIRK5K13AR14A double mutant, were localized to the ER and the plasma membrane of the vegetal pole of the oocyte, respectively. Silencing of GIRK5 or blocking of this channel by external barium prevented progesterone‐induced meiotic progression. The endogenous level of GIRK5 protein decreased through oocyte stages in prophase I augmenting by progesterone. In conclusion, we have identified a unique mechanism by which the expression pattern of a K(+) channel evolved to control Xenopus oocyte maturation. John Wiley and Sons Inc. 2021-03-03 /pmc/articles/PMC8016131/ /pubmed/33565726 http://dx.doi.org/10.1002/2211-5463.13113 Text en © 2021 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Rangel‐Garcia, Claudia I.
Salvador, Carolina
Chavez‐Garcia, Karla
Diaz‐Bello, Beatriz
Lopez‐Gonzalez, Zinaeli
Vazquez‐Cruz, Lourdes
Angel Vazquez‐Martinez, Julio
Ortiz‐Navarrete, Vianney
Riveros‐Rosas, Hector
Escobar, Laura I.
Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation
title Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation
title_full Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation
title_fullStr Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation
title_full_unstemmed Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation
title_short Identification of a unique endoplasmic retention motif in the Xenopus GIRK5 channel and its contribution to oocyte maturation
title_sort identification of a unique endoplasmic retention motif in the xenopus girk5 channel and its contribution to oocyte maturation
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8016131/
https://www.ncbi.nlm.nih.gov/pubmed/33565726
http://dx.doi.org/10.1002/2211-5463.13113
work_keys_str_mv AT rangelgarciaclaudiai identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT salvadorcarolina identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT chavezgarciakarla identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT diazbellobeatriz identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT lopezgonzalezzinaeli identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT vazquezcruzlourdes identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT angelvazquezmartinezjulio identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT ortiznavarretevianney identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT riverosrosashector identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration
AT escobarlaurai identificationofauniqueendoplasmicretentionmotifinthexenopusgirk5channelanditscontributiontooocytematuration