Q. Hu et al., IDENTIFICATION OF RLK, A NOVEL PROTEIN-TYROSINE KINASE WITH PREDOMINANT EXPRESSION IN THE T-CELL LINEAGE, The Journal of biological chemistry, 270(4), 1995, pp. 1928-1934
The control of phosphorylation by protein tyrosine kinases represents
an important regulatory mechanism in T cell growth, function, and diff
erentiation. We have identified a 62-kDa murine protein tyrosine kinas
e predominantly expressed within the T cell lineage, which we have ter
med Rlk (for Resting lymphocyte kinase), rlk mRNA was found to be expr
essed in the fetal thymus as early as day 13 of embryonic development
as well as in adult thymus and mature resting peripheral T cells, The
sequence of rlk showed that it is most closely related to the subfamil
y of cytoplasmic tyrosine kinases that includes the Btk, Itk, and Tec
proteins. However, Rlk differs from these kinases by virtue of its uni
que aminoterminal domain, which lacks a region of pleckstrin homology
common to the other members of this protein subfamily. Examination of
rlk abundance within different T cell subpopulations revealed preferen
tial expression in Th1 relative to Th2 T cell clones, suggesting a pos
sible role in signal transduction pathways that selectively regulate c
ytokine production in mature CD4(+) T cell subsets. Rlk thus represent
s a novel cytoplasmic tyrosine kinase with potential functions in intr
athymic T cell development and mature T cell signaling.