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J. Biol. Chem., Vol. 269, Issue 49, 30808-30817, 12, 1994
LB Holzman, SE Merritt and G Fan
Molecular cloning using a degenerate oligonucleotide-based polymerase chain
reaction was undertaken to test the possibility that novel, developmentally
regulated protein kinases are expressed in the embryonic mouse kidney.
Several receptor tyrosine kinase and serine/threonine kinase cDNA clones
were identified. One of these, designated DLK, represented a novel gene
product whose 3.6-kilobase transcript was expressed in a tissue-specific
and developmentally regulated fashion. Several clones encoding the entire
open reading frame were isolated and sequenced. The identified open reading
frame encodes an 888-amino acid polypeptide that defines a new subfamily
within the mixed lineage protein kinase family. Sequence analysis revealed:
1) a kinase catalytic domain most characteristic of serine/threonine
kinases but hybrid between members of the family of microtubule-associated
protein kinase kinase kinases and the fibroblast growth factor receptor
family; 2) two putative alpha-helical leucine zipper motifs separated by a
25-amino acid charged intermediate segment but lacking an NH2-terminal
basic domain; and 3) COOH-terminal and NH2- terminal proline-rich domains
suggestive of src homology 3 (SH3) domain binding regions. Rabbit
polyclonal immune sera generated against a carboxyl-terminal bacterial
fusion protein recognized a protein with an apparent molecular mass of 130
kDa in COS 7 cells that were transiently transfected with a full-length DLK
cDNA expression vector. Moreover, COS 7 cells transiently transfected with
an epitope-tagged DLK expression vector expressed protein with an apparent
molecular mass of 130 kDa that became autophosphorylated on serine and
threonine in an in vitro kinase assay.
Identification, molecular cloning, and characterization of dual leucine zipper bearing kinase. A novel serine/threonine protein kinase that defines a second subfamily of mixed lineage kinases
Department of Internal Medicine, University of Michigan Medical School, Ann Arbor 48109-0676.
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