ArticleThe Biochemical journal1998
Selective loss of substrate recognition induced by the tumour-associated D294G point mutation in protein kinase Calpha.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- The complexities of PKCα signaling in cancer.Advances in biological regulation · 2021Review
- Article
- Protein kinase signaling networks in cancer.Current opinion in genetics & development · 2011Review
- A spatiotemporally coordinated cascade of protein kinase C activation controls isoform-selective translocation.Molecular and cellular biology · 2006Article
- A single point mutation in the V3 region affects protein kinase Calpha targeting and accumulation at cell-cell contacts.Molecular and cellular biology · 2001Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tumour-associated D294G mutant of protein kinase Calpha (PKCalpha) was recently shown not to be translocated to the plasma membrane on stimulation with PMA, in contrast with the wild-type enzyme. Using recombinant wild-type and mutant PKCalpha, we establish here that, although the PKCalpha intrinsic lipid-dependent catalytic activity remains unaltered by the D294G mutation, the mutant enzyme exhibits a selective loss of substrate recognition. Indeed, whereas the mutant enzyme is still able to phosphorylate histone IIIS with comparable efficiency to that of the wild-type enzyme, it exhibits a lack of kinase activity towards the previously cloned 35F and 35H substrates for PKC. Overlay experiments demonstrate that this selective loss of kinase activity is correlated with a decrease in binding of D294G PKCalpha to the 35F and 35H proteins compared with that of the wild-type enzyme. Because the 35H and 35F proteins are predicted to be PKCalpha-anchoring proteins, these findings suggest a selective loss of PKCalpha-protein interactions that might fail to stabilize the location of the PKCalpha mutant at the plasma membrane.
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