High impact information on Pkc53E

• One, dPKC98F, maps to chromosome region 98F and displays over 60% amino acid sequence identity with members of a recently described "PKC-related" subfamily in mammals [1].
• Furthermore, this synthetic lethality was caused by the incapability of RhoA to activate Pkc1p, but not glucan synthase [2].
• We found that PKMzeta accumulated in neurofibrillary tangles (NFTs), whereas conventional and novel PKC isoforms did not [3].
• Protein kinase Mzeta (PKMzeta), an atypical protein kinase C (PKC) isoform, plays a key role in the maintenance of long-term potentiation (LTP), a persistent enhancement of AMPA receptor-mediated synaptic transmission, as well as in the persistence of memory in Drosophila [3].
• To determine whether other protein kinases use a similar mechanism to activate the enzyme, the effects of protein kinase C mediated phosphorylation on the individual steps of the topoisomerase II catalytic cycle were assessed [4].

Biological context of Pkc53E

• The genes contain six (T. reesei) and eight (A. niger) introns, which exhibit notable conservation in position with those found in the corresponding Schizosaccharomyces pombe pkc1+ and Drosophila melanogaster dPKC53Ebr genes [5].
• Inhibition of PKC activity by protein kinase inhibitors blocked USP phosphorylation, resulting in inhibition of 20E-induced gene expression at both transcriptional and translational levels [6].

Anatomical context of Pkc53E

• PKC-mediated USP phosphorylation is required for 20E-induced gene expression in the salivary glands of Drosophila melanogaster [6].
• The Ca2+-dependent protein kinase C (PKC) isoform PKCalpha plays a crucial role in initiating endothelial cell contraction and disassembly of VE-cadherin junctions [7].

Analytical, diagnostic and therapeutic context of Pkc53E

• A polyclonal antiserum raised against the pseudosubstrate-binding domain of PKC1 recognizes in T. reesei a 115-120 kDa protein in Western blots [5].

References