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- W2090920875 abstract "PCTAIRE kinases (PCTK) are a highly conserved, but poorly characterized, subgroup of cyclin-dependent kinases (CDK). They are characterized by a conserved catalytic domain flanked by N- and C-terminal extensions that are involved in cyclin binding. Vertebrate genomes contain three highly similar PCTAIRE kinases (PCTK1,2,3, a.k.a., CDK16,17,18), which are most abundant in post-mitotic cells in brain and testis. Consistent with this restricted expression pattern, PCTK1 (CDK16) has recently been shown to be essential for spermatogenesis. PCTAIREs are activated by cyclin Y (CCNY), a highly conserved single cyclin fold protein. By binding to N-myristoylated CCNY, CDK16 is targeted to the plasma membrane. Unlike conventional cyclin-CDK interactions, binding of CCNY to CDK16 not only requires the catalytic domain, but also domains within the N-terminal extension. Interestingly, phosphorylation within this domain blocks CCNY binding, providing a novel means of cyclin-CDK regulation. By using these functional characteristics, we analyzed PCTAIRE sequence containing protein kinase genes in genomes of various organisms and found that CCNY and CCNY-dependent kinases are restricted to eumetazoa and possibly evolved along with development of a central nervous system. Here, we focus on the structure and regulation of PCTAIREs and discuss their established functions." @default.
- W2090920875 created "2016-06-24" @default.
- W2090920875 creator A5004826028 @default.
- W2090920875 creator A5069887691 @default.
- W2090920875 creator A5091902984 @default.
- W2090920875 date "2012-08-16" @default.
- W2090920875 modified "2023-10-01" @default.
- W2090920875 title "Orphan kinases turn eccentric" @default.
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- W2090920875 doi "https://doi.org/10.4161/cc.21592" @default.
- W2090920875 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3495819" @default.
- W2090920875 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22895054" @default.
- W2090920875 hasPublicationYear "2012" @default.
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