Synthesis and phorbol ester-binding studies of the individual cysteine-rich motifs of protein Kinase D
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Cited by (16)
Potein kinase D signaling in cancer: A friend or foe?
2017, Biochimica et Biophysica Acta - Reviews on CancerCitation Excerpt :Overall, C1 domain is central to the spatial and temporal regulation of PKD localization at different subcellular locations. In addition to the intrinsic differences of the twin C1 domains [20,24,25], their ligand binding activity, selectivity, and accessibility to ligand in a holoenyme are intricately regulated by PKD phosphorylation [22], kinase activity [19,21,22] and interactions with protein binding partners [26], and this regulation becomes more complex with embedded nuclear localization and export signals within the structure of C1 domain [27]. Whether, how, and how much they contribute to the differential biological functions of PKD isoforms remain to be determined.
Synthesis and phorbol ester binding of the cysteine-rich domains of diacylglycerol kinase (DGK) isozymes. DGKγ and DGKβ are new targets of tumor-promoting phorbol esters
2003, Journal of Biological ChemistryCitation Excerpt :These peptides were folded using zinc chloride by a method reported previously (23, 24) and subjected to a PDBu binding assay. Because our recent investigation found that some C1 domain fragments of PKC isozymes suffered from temperature-dependent inactivation (24, 33), the incubation temperature of the binding assay was set at 4 °C for the DGK isozyme C1 peptides. The specific binding to PDBu of the DGK C1 peptides is summarized in Fig.3.
Mechanism of persistent protein kinase D1 translocation and activation
2003, Developmental CellDiacylglycerol kinase γ is one of the specific receptors of tumor-promoting phorbol esters
2001, Biochemical and Biophysical Research Communications