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Vol. 62, Issue 1, 65-74, July 2002
Superfamily Type I Activin Receptor-Like Kinase (ALK)
Receptors ALK4, ALK5, and ALK7
Laboratory of Developmental Signalling, Cancer Research UK London
Research Institute, Lincoln's Inn Fields Laboratories, London, UK
(G.J.I., F.J.N., C.S.H.); Department of Medicinal Chemistry,
GlaxoSmithKline Pharmaceuticals, Collegeville, Pennsylvania (J.F.C.);
Department of Medicinal Chemistry, GlaxoSmithKline Pharmaceuticals,
Stevenage, Hertfordshire, UK (J.D.H.); Department of High-Throughput
Chemistry (L.M.G.) and High-Throughput Biology (A.D.R.),
GlaxoSmithKline Pharmaceuticals, Harlow, Essex, UK; and Renal and
Urology Research, GlaxoSmithKline Pharmaceuticals, King of Prussia,
Pennsylvania (N.J.L.)
Small molecule inhibitors have proven extremely useful for
investigating signal transduction pathways and have the potential for
development into therapeutics for inhibiting signal transduction pathways whose activities contribute to human diseases. Transforming growth factor 
(TGF-) is a member of a large family of
pleiotropic cytokines that are involved in many biological processes,
including growth control, differentiation, migration, cell survival,
adhesion, and specification of developmental fate, in both normal and
diseased states. TGF- superfamily members signal through a receptor
complex comprising a type II and type I receptor, both
serine/threonine kinases. Here, we characterize a small molecule
inhibitor (SB-431542) that was identified as an inhibitor of
activin receptor-like kinase (ALK)5 (the TGF- type I
receptor). We demonstrate that it inhibits ALK5 and also the activin
type I receptor ALK4 and the nodal type I receptor ALK7, which are very
highly related to ALK5 in their kinase domains. It has no effect on the
other, more divergent ALK family members that recognize bone
morphogenetic proteins (BMPs). Consistent with this, we demonstrate
that SB-431542 is a selective inhibitor of endogenous activin and
TGF- signaling but has no effect on BMP signaling. To demonstrate
the specificity of SB-431542, we tested its effect on several other
signal transduction pathways whose activities depend on the concerted
activation of multiple kinases. SB-431542 has no effect on components
of the ERK, JNK, or p38 MAP kinase pathways or on components of the
signaling pathways activated in response to serum.
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