Article

Pearson, R. B. & Kemp, B. E. Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 200, 62-81

Methods in Enzymology (Impact Factor: 2.19). 02/1991; 200:62-81. DOI: 10.1016/0076-6879(91)00127-I
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    • "Since phosphorylation of ribosomal S6 is thought to be specific to TORC1 signalling, we decided to look further into its phosphorylation. It has previously been demonstrated that the anti-PAS antibody, which recognises phosphorylation of the [R/ K]X[R/K]XX[S/T] consensus motif in mammalian S6K1 and other AGC kinase substrates (Manning et al., 2002; Pearson and Kemp, 1991) (Cell Signalling Technology), detects phosphorylation of fission yeast Rps6 serine 235 (Nakashima et al., 2010). Ribosomal S6 is encoded by two genes in fission yeast: rps601 and rps602. "
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    Biology Open 09/2012; 1(9):884-8. DOI:10.1242/bio.20122022 · 2.42 Impact Factor
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    • "Multiplexed analysis permits synchronous, parallelized multiple sampling and testing from the same tissue lysate, thus making it a powerful analytical tool. In addition to biochemical measures of phosphate incorporation using ATP as a substrate, a number of high-throughput methods generally using antibody detection of phosphopeptide products have been perfected [5] [7] [8]. Recently, interest has shifted to inhibitors with an appropriate pattern of kinase inhibition that includes several kinases as the target [10]. "
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    • "Recently, also the nonhuman herpesvirus Pseudorabies Virus (PRV) U S 3 kinase was shown to induce phosphorylation of HDAC2 on serine 407, indicating a conserved effect of many herpesviruses on this deacetylase [58]. The kinase(s) directly responsible for HDAC1 and HDAC2 phosphorylations in vivo is unknown; CKII seems unlikely to be the cellular kinase involved, since it requires the acidic consensus sequence S/T- X-X-E [59], not present in the region encompassing serines 406 of HDAC1 and 407 of HDAC2. CKII-dependent phosphorylation of HDAC1 and HDAC2 is also increased in response to hypoxic conditions, and this correlates with an increase in HDAC enzymatic activity [60]. "
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    ABSTRACT: Class I histone deacetylases (HDACs) are cellular enzymes expressed in many tissues and play crucial roles in differentiation, proliferation, and cancer. HDAC1 and HDAC2 in particular are highly homologous proteins that show redundant or specific roles in different cell types or in response to different stimuli and signaling pathways. The molecular details of this dual regulation are largely unknown. HDAC1 and HDAC2 are not only protein modifiers, but are in turn regulated by post-translational modifications (PTMs): phosphorylation, acetylation, ubiquitination, SUMOylation, nitrosylation, and carbonylation. Some of these PTMs occur and crosstalk specifically on HDAC1 or HDAC2, creating a rational "code" for a differential, context-related regulation. The global comprehension of this PTM code is central for dissecting the role of single HDAC1 and HDAC2 in physiology and pathology.
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