Phosphorylation is an important type of protein post-translational modification. Identification of possible phosphorylation sites of a protein is important for understanding its functions. Unbiased screening for phosphorylation sites by in vitro or in vivo experiments is time consuming and expensive; in silico prediction can provide functional candidates and help narrow down the experimental ef...

Cortactin is a scaffolding protein that is targeted to sites of actin polymerization, including lamellipodia in migrating cells, cell-cell junctions in epithelial cells, growth cones of neurons, podosomes of osteoclasts, invadopodia of tumor cells, and sites of actin rearrangement induced by pathogenic bacteria and viruses (Daly, 2004; Lua and Low, 2005; Pfaff and Jurdic, 2001). Although it is ...

MOTIVATION Kinase-mediated phosphorylation is the central mechanism of post-translational modification to regulate cellular responses and phenotypes. Signaling defects associated with protein phosphorylation are linked to many diseases, particularly cancer. Characterizing protein kinases and their substrates enhances our ability to understand and treat such diseases and broadens our knowledge o...

PhosphoBase is a database of experimentally verified phosphorylation sites. Version 1.0 contains 156 entries and 398 experimentally determined phosphorylation sites. Entries are compiled and revised from the literature and from major protein sequence databases such as SwissProt and PIR. The entries provide information about the phosphoprotein and the exact position of its phosphorylation sites....

Rapid desensitization of G protein-coupled receptors is mediated, at least in part, by their phosphorylation by the G protein-coupled receptor kinases (GRKs). However, only in the case of rhodopsin have the actual sites of receptor phosphorylation been unambiguously determined. Although previous studies have implicated the cytoplasmic tail of the b2-adrenergic receptor (b2AR) as the site of GRK...

ABSTRACT The C-terminal of G protein-coupled receptors is now recognized as being important for protein activation and signaling function. To detect the role tail in receptor activation, we used α1b-AR, which has a long 164 amino acids. We constructed intramolecular FRET sensors, was truncated to 10 (∆C-10), 20 (∆C-20), 30 (∆C-30), 50 (∆C-50), 70 (∆C-70), or 90 (∆C-90). mutants ∆C-10, ∆C-20, ∆C...

Control of the translational repressor, PHAS-I, was investigated by expressing proteins with Ser/Thr --> Ala mutations in the five (S/T)P phosphorylation sites. Results of experiments with HEK293 cells reveal at least three levels of control. At one extreme is nonregulated phosphorylation, exemplified by constitutive phosphorylation of Ser82. At an intermediate level, amino acids and insulin st...

Protein phosphorylation/dephosphorylation is the central mechanism of post-translational modification which regulates cellular responses and phenotypes. Due to the efficiency and resource constraints of the in vivo methods for identifying phosphorylation sites, there is a strong motivation to computationally predict potential phosphorylation sites. In this work, we propose to use a unique set o...

Reversible protein phosphorylation provides a major regulatory mechanism in eukaryotic cells. Due to the high variability of amino acid residues flanking a relatively limited number of experimentally identified phosphorylation sites, reliable prediction of such sites still remains an important issue. Here we report the development of a new web-based tool for the prediction of protein phosphoryl...

Protein kinase C (PKC) phosphorylates the regulatory light chains of smooth muscle and cytoplasmic myosin II at three known sites: S1, S2, and T9 [Ikebe, M., Hartshorne, D. J., & Elzinga, M. (1987) J. Biol. Chem. 262, 9569-9573]. Phosphorylation at these sites inhibits the actomyosin ATPase and inhibits phosphorylation of S19 on the regulatory light chain by myosin light chain kinase (MLCK) [Ni...