Cargando…
Massive Autophosphorylation of the Ser/Thr-Rich Domain Controls Protein Kinase Activity of TRPM6 and TRPM7
TRPM6 and TRPM7 are bifunctional proteins expressing a TRP channel fused to an atypical α-kinase domain. While the gating properties of TRPM6 and TRPM7 channels have been studied in detail, little is known about the mechanisms regulating kinase activity. Recently, we found that TRPM7 associates with...
Autores principales: | Clark, Kristopher, Middelbeek, Jeroen, Morrice, Nick A., Figdor, Carl G., Lasonder, Edwin, van Leeuwen, Frank N. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2267223/ https://www.ncbi.nlm.nih.gov/pubmed/18365021 http://dx.doi.org/10.1371/journal.pone.0001876 |
Ejemplares similares
-
Autophosphorylation Mechanism of the Ser/Thr Kinase Stk1 From Staphylococcus aureus
por: Zheng, Weihao, et al.
Publicado: (2018) -
TRPM7 maintains progenitor-like features of neuroblastoma cells: implications for metastasis formation
por: Middelbeek, Jeroen, et al.
Publicado: (2015) -
Functional analysis of the BRI1 receptor kinase by Thr-for-Ser substitution in a regulatory autophosphorylation site
por: Oh, Man-Ho, et al.
Publicado: (2015) -
Expression of TRPM6 and TRPM7 in the preterm piglet heart
por: Forbes, Elizabeth M., et al.
Publicado: (2022) -
Involvement of TRPM2 and TRPM8 in temperature-dependent masking behavior
por: Ota, Wataru, et al.
Publicado: (2019)