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• W2005012362 abstract "Three different genes of catalytic subunit A of the Ca2+-dependent serine/threonine protein phosphatase calcineurin (CaN) are encoded in the human genome forming heterodimers with regulatory subunit B. Even though physiological roles of CaN have been investigated extensively, less is known about the specific functions of the different catalytic isoforms. In this study, all human CaN holoenzymes containing either the α, β, or γ isoform of the catalytic subunit (CaN α, β, or γ, respectively) were expressed for the first time. Comparative kinetic analysis of the dephosphorylation of five specific CaN substrates provided evidence that the distinct isoforms of the catalytic subunit confer substrate specificities to the holoenzymes. CaN α dephosphorylates the transcription factor Elk-1 with 7- and 2-fold higher catalytic efficiencies than the β and γ isoforms, respectively. CaN γ exhibits the highest kcat/Km value for DARPP-32, whereas the catalytic efficiencies for the dephosphorylation of NFAT and RII peptide were 3- and 5-fold lower, respectively, when compared with the other isoforms. Elk-1 and NFAT reporter gene activity measurements revealed even more pronounced substrate preferences of CaNA isoforms. Moreover, kinetic analysis demonstrated that CaN β exhibits for all tested protein substrates the lowest Km values. Enzymatic characterization of the CaN βP14G/P18G variant as well as the N-terminal truncated form CaN β22−524 revealed that the proline-rich sequence of CaN β is involved in substrate recognition. CaN β22−524 exhibits an at least 4-fold decreased substrate affinity and a 5-fold increased turnover number. Since this study demonstrates that all CaN isoforms display the same cytoplasmic subcellular distribution and are expressed in each tested cell line, differences in substrate specificities may determine specific physiological functions of the distinct isoforms." @default.
• W2005012362 created "2016-06-24" @default.
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• W2005012362 date "2009-01-20" @default.
• W2005012362 modified "2023-10-18" @default.
• W2005012362 title "The Proline-Rich N-Terminal Sequence of Calcineurin Aβ Determines Substrate Binding" @default.
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• W2005012362 doi "https://doi.org/10.1021/bi8019355" @default.
• W2005012362 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19154138" @default.
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