Developmental expression of pim kinases suggests functions also outside of the hematopoietic system

A Eichmann, L Yuan, C Bréant, K Alitalo, PÈJ Koskinen - Oncogene, 2000 - nature.com
A Eichmann, L Yuan, C Bréant, K Alitalo, PÈJ Koskinen
Oncogene, 2000nature.com
We have cloned a novel quail cDNA with strong homology to the pim family of proto-
oncogenes. The deduced amino acid (aa) sequence of the cDNA, named qpim, is more
closely related to Xenopus Pim and to the recently identified rat Pim-3 than to human or
rodent Pim-1 or Pim-2. The protein encoded by the qpim cDNA can autophosphorylate itself
and share substrates with murine Pim-1, suggesting functional redundancy to other Pim
family serine/threonine kinases. We have compared the expression of qpim in avian …
Abstract
We have cloned a novel quail cDNA with strong homology to the pim family of proto-oncogenes. The deduced amino acid (aa) sequence of the cDNA, named qpim, is more closely related to Xenopus Pim and to the recently identified rat Pim-3 than to human or rodent Pim-1 or Pim-2. The protein encoded by the qpim cDNA can autophosphorylate itself and share substrates with murine Pim-1, suggesting functional redundancy to other Pim family serine/threonine kinases. We have compared the expression of qpim in avian embryos to mouse pim-1,-2 and-3 by in situ hybridization. qpim shows a highly dynamic expression pattern, particularly at early developmental stages. Surprisingly, its expression pattern is not identical to any of the murine pim genes, which show complementary and/or partially overlapping expression sites both in-and outside of the hematopoietic system. Altogether, our results suggest novel functions for Pim family kinases during embryonic development, in particular in epithelia and in the central nervous system.
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