Publication:

C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity

Date

Date

Date
2018
Journal Article
Published version

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Citation copied

Murillo-de-Ozores, A. R., Rodríguez-Gama, A., Bazúa-Valenti, S., Leyva-Ríos, K., Vázquez, N., Pacheco-Álvarez, D., De La Rosa-Velázquez, I. A., Wengi, A., Stone, K. L., Zhang, J., Loffing, J., Lifton, R. P., Yang, C.-L., Ellison, D. H., Gamba, G., & Castañeda-Bueno, M. (2018). C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity. Journal of Biological Chemistry, 293(31), 12209–12221. https://doi.org/10.1074/jbc.RA118.003037

Abstract

Abstract

Abstract

WNK lysine-deficient protein kinase 4 (WNK4) is an important regulator of renal salt handling. Mutations in its gene cause pseudohypoaldosteronism type II, mainly arising from overactivation of the renal Na+/Cl- cotransporter (NCC). In addition to full-length WNK4, we have observed faster migrating bands (between 95 and 130 kDa) in Western blots of kidney lysates. Therefore, we hypothesized that these could correspond to uncharacterized WNK4 variants. Here, using several WNK4 antibodies and WNK4-/- mice as controls, we showed that the

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33 since deposited on 2019-03-07
Acq. date: 2025-11-12

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64 since deposited on 2019-03-07
Acq. date: 2025-11-12

Additional indexing

Creators (Authors)

  • Murillo-de-Ozores, Adrián Rafael
    affiliation.icon.alt
  • Rodríguez-Gama, Alejandro
    affiliation.icon.alt
  • Bazúa-Valenti, Silvana
    affiliation.icon.alt
  • Leyva-Ríos, Karla
    affiliation.icon.alt
  • Vázquez, Norma
    affiliation.icon.alt
  • Pacheco-Álvarez, Diana
    affiliation.icon.alt
  • De La Rosa-Velázquez, Inti A
    affiliation.icon.alt
  • Wengi, Agnieszka
    affiliation.icon.alt
  • Stone, Kathryn L
    affiliation.icon.alt
  • Zhang, Junhui
    affiliation.icon.alt
  • Loffing, Johannes
    affiliation.icon.alt
  • Lifton, Richard P
    affiliation.icon.alt
  • Yang, Chao-Ling
    affiliation.icon.alt
  • Ellison, David H
    affiliation.icon.alt
  • Gamba, Gerardo
    affiliation.icon.alt
  • Castañeda-Bueno, Maria
    affiliation.icon.alt

Journal/Series Title

Journal/Series Title

Journal/Series Title

Volume

Volume

Volume
293

Number

Number

Number
31

Page range/Item number

Page range/Item number

Page range/Item number
12209

Page end

Page end

Page end
12221

Item Type

Item Type

Item Type
Journal Article

Dewey Decimal Classifikation

Dewey Decimal Classifikation

Dewey Decimal Classifikation

Language

Language

Language
English

Publication date

Publication date

Publication date
2018-08-03

Date available

Date available

Date available
2019-03-07

ISSN or e-ISSN

ISSN or e-ISSN

ISSN or e-ISSN
0021-9258

OA Status

OA Status

OA Status
Hybrid

Free Access at

Free Access at

Free Access at
Pubmed ID

PubMed ID

PubMed ID

PubMed ID

Metrics

Downloads

33 since deposited on 2019-03-07
Acq. date: 2025-11-12

Views

64 since deposited on 2019-03-07
Acq. date: 2025-11-12

Citations

Citation copied

Murillo-de-Ozores, A. R., Rodríguez-Gama, A., Bazúa-Valenti, S., Leyva-Ríos, K., Vázquez, N., Pacheco-Álvarez, D., De La Rosa-Velázquez, I. A., Wengi, A., Stone, K. L., Zhang, J., Loffing, J., Lifton, R. P., Yang, C.-L., Ellison, D. H., Gamba, G., & Castañeda-Bueno, M. (2018). C-terminally truncated, kidney-specific variants of the WNK4 kinase lack several sites that regulate its activity. Journal of Biological Chemistry, 293(31), 12209–12221. https://doi.org/10.1074/jbc.RA118.003037

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