Cargando…
Binding of smoothelin-like 1 to tropomyosin and calmodulin is mutually exclusive and regulated by phosphorylation
BACKGROUND: The smoothelin-like 1 protein (SMTNL1) can associate with tropomyosin (Tpm) and calmodulin (CaM), two proteins essential to the smooth muscle contractile process. SMTNL1 is phosphorylated at Ser301 by protein kinase A during calcium desensitization in smooth muscle, yet the effect of SMT...
Autores principales: | Ulke-Lemée, Annegret, Sun, David Hao, Ishida, Hiroaki, Vogel, Hans J., MacDonald, Justin A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5359911/ https://www.ncbi.nlm.nih.gov/pubmed/28320308 http://dx.doi.org/10.1186/s12858-017-0080-6 |
Ejemplares similares
-
Mapping and functional characterization of the murine Smoothelin-like 1 promoter
por: Ulke-Lemée, Annegret, et al.
Publicado: (2011) -
Tools and protocol for quantification of myosin phosphorylation with MRM-MS
por: MacDonald, Justin A., et al.
Publicado: (2018) -
Opportunities to Target Specific Contractile Abnormalities with Smooth Muscle Protein Kinase Inhibitors
por: Ulke-Lemée, Annegret, et al.
Publicado: (2010) -
Smoothelin-like 1 deletion enhances myogenic reactivity of mesenteric arteries with alterations in PKC and myosin phosphatase signaling
por: Turner, Sara R., et al.
Publicado: (2019) -
Overexpression of human fibroblast caldesmon fragment containing actin- , Ca++/calmodulin-, and tropomyosin-binding domains stabilizes endogenous tropomyosin and microfilaments
Publicado: (1994)