Threonine-497 is a critical site for permissive activation of protein kinase Cα
نویسندگان
چکیده
منابع مشابه
Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase Cα
BACKGROUND It has been widely reported that multisite phosphorylation plays an essential role in the regulation of protein kinases. However, our understanding of how these events modify protein function in vitro and in vivo is poorly understood. Protein kinase C (PKC) affords an interesting example of how phosphorylation control is coupled to effector control. PKC is acutely regulated by the se...
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DnaK, the sole Escherichia coli member of the highly conserved 70-kDa heat shock protein (HSP70) family of proteins, autophosphorylates when incubated with ATP in vitro. We show that threonine-199 is the amino acid that becomes phosphorylated and we demonstrate that threonine-199 is critical for the ATPase activity of DnaK. We also report that both the ATPase and autophosphorylating activities ...
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Previously, we showed caveolae contain a population of protein kinase Calpha (PKCalpha) that appears to regulate membrane invagination. We now report that multiple PKC isoenzymes are enriched in caveolae of unstimulated fibroblasts. To understand the mechanism of PKC targeting, we prepared caveolae lacking PKCalpha and measured the interaction of recombinant PKCalpha with these membranes. PKCal...
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Fc receptors play a pivotal role linking the cellular the mechanisms regulating receptor coupling to PLD in intact cells where the components are endogenously ex-and humoral arms of the immune system [1–3]. Our previous studies have shown that the human high-pressed and functional. First, the presence of specific PLD isozymes in the cell membrane fraction was exam-affinity immunoglobulin G rece...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3010443