Related Experiment Video
Updated: Jul 2, 2026

Pull-down of Calmodulin-binding Proteins
Published on: January 23, 2012
Effects of calmodulin and calmodulin binding protein BP-10 on phosphorylation of thylakoid membrane protein
1Department of Biochemistry and Molecular Biology, Nankai University, Tianjin, China.
Abstract:
Light-induced phosphorylation of endogenous thylakoid membrane protein can be inhibited markedly by a novel inhibitor CaMBP-10 which is discovered and isolated from plant. The inhibitory effect of BP-10 can be eliminated by addition of CaM. At the same time, the phosphorylation can also be inhibited by EGTA or CaM antagonists, such as TFP (trifluoperazine) and W-7 (N-(6-aminohexyl)-5-chloro-l-naphthalene sulfonamide). This result implies that (i) Ca(2+) and CaM most likely participate in and regulate plant photosynthesis; (ii) the kinase that catalyzes thylakoid membrane protein phosphorylation can be regulated by Ca(2+) and CaM. However, the further experiments indicate that BP-10 has no effect on dephosphorylation of thylakoid phosphoproteins.
Related Concept Videos
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Amplifying Signals via Enzymatic Cascade
IP3/DAG Signaling Pathway

