Phosphor ylated Pim1
Phosphor ylated Pim1: Human Proviral Integration Site for MulV phosphorylated at Ser261
PDB Code: 2BIK
The structure of un-phosphorylated Pim1 revealed that this kinase is in an active conformation in the absence of phosphorylated residues in the activation loop. However, Pim1 auto-phosphorylates rapidly in vitro and auto-phosphorylation sites for the highly homologues Xenopus Pim1 has been mapped to the activation loop residues Ser190 and Thr205.
We found that human Pim1 is highly phosphorylated after heterologous expression in E.coli . We were able to purify a mono-phosphorylated form of Pim1 and determined the structure of this enzyme at 1.8 Å resolution. The electron density map showed that the phosphate moiety is located on residue Ser261 which is situated in the lower kinase lobe close to the C-terminus of the protein. However, mapping of auto-phosphorylation sites generated using completely un-phosphorylated Pim1 revealed that this side is not phosphorylated by Pim1 in vitro . Instead, two other phosphorylation sites were detected in ESI-MS spectra. The first site, which showed rapid auto-phosphorylation kinetics was mapped to Ser8 (MLLSK INS*LAHLR) located in the unstructured N-terminus of Pim1. The N-terminus of Pim has been shown to be important for several Pim interacting proteins like CDC25. It is therefore likely that phosphorylation at Ser8 plays a role in modulating these interactions. The second auto-phosphorylation site detected in ESI-MS spectra was not mapped. However, the slow auto-phosphorylation kinetics measured for this site makes it unlikely that this site will play a role modulating Pim function in vivo due to the short half life of this enzyme. Taken together the auto-phosphorylation studies carried out show that human Pim1 kinase activity is not influenced by auto-phosphorylation of activation loop residues.
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