Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Regular paperAnalysis of the in vivo phosphorylation state of protein phosphatase inhibitor-2 from rabbit skeletal muscle by fast-atom bombardment mass spectrometry
References (24)
- et al.
FEBS Lett.
(1979) - et al.
FEBS Lett.
(1982) J. Biol. Chem.
(1984)- et al.
Biochim. Biophys. Acta
(1986) - et al.
FEBS Lett.
(1986) FEBS Lett.
(1987)- et al.
FEBS Lett.
(1986) - et al.
Eur. J. Biochem.
(1976) - et al.
Biochemistry
(1983) - et al.
Eur. J. Biochem.
(1984)
Eur. J. Biochem.
Eur. J. Biochem.
Cited by (42)
Regulation of protein phosphatase 1<inf>I</inf> by Cdc25C-Associated kinase 1 (C-TAK1) and PFTAIRE protein kinase
2014, Journal of Biological ChemistryCitation Excerpt :However, it is important to point out that direct evidence for phosphorylation of Thr-72 of I-2 in vivo is limited. Analysis of rabbit skeletal muscle I-2 by fast atom bombardment mass spectrometry revealed only serine phosphorylation (41). This has been corroborated by immunoprecipitation of I-2 extracts also showing that 90–95% of phosphorylation was on seryl residues (42).
Chapter 5 Phosphorylation-specific analysis strategies for mass spectrometry: enhanced detection of phosphorylated proteins and peptides
2005, Comprehensive Analytical ChemistryCitation Excerpt :However, labeling of phosphoproteins with radioactive [32/33P]phosphate is required and the amount of protein needed for the latter experiments far exceeds the levels needed for MS-based strategies. MS was first applied for assignment of phosphorylation sites using fast-atom bombardment ionization MS (FAB-MS); 252Cf plasma desorption MS (PD-MS); liquid secondary ion MS (LSI-MS) and sector mass analyzers [41,52,60,95,191,195,218]. Sample size requirements of mass spectrometers using these ionization techniques were in the nanomole level, often exceeding the amount of material available, practically, from biological samples.
Neuronal Cdc2-like Protein Kinase (Cdk5/p25) Is Associated with Protein Phosphatase 1 and Phosphorylates Inhibitor-2
2001, Journal of Biological ChemistryCitation Excerpt :These observations suggest that phosphorylation of I-2 by NCLK within the PP1·I-2 complex is also a transient event. I-2 is phosphorylated on Ser86, Ser120, and Ser121 in vivo (36), and these sites are phosphorylated by CK2 in vitro (1, 37). CK2 phosphorylation does not activate PP1·I-2 but enhances Thr72phosphorylation by GSK3 (8, 9).
Regulation of protein phosphatase-1
2000, Chemistry and BiologyProtein phosphorylation: Technologies for the identification of phosphoamino acids
1998, Journal of Chromatography A
- ∗
Present address: Department of Biochemistry, University of Washington, Seattle, WA 98195, U.S.A.