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Vol. 13, Issue 12, 4484-4496, December 2002
Receptor-interacting
Protein That Is Also a Light Chain of the Motor Protein Dynein
*Department of Pharmacology and §Intercollege Graduate
Program in Genetics, Pennsylvania State University College of Medicine,
Hershey, Pennsylvania 17033
The phosphorylated, activated cytoplasmic domains of the
transforming growth factor-
(TGF) receptors were used as probes to screen an expression library that was prepared from a highly TGF-responsive intestinal epithelial cell line. One of the TGF receptor-interacting proteins isolated was identified to be the mammalian homologue of the LC7 family (mLC7) of dynein light chains (DLCs). This 11-kDa cytoplasmic protein interacts with the
TGF receptor complex intracellularly and is phosphorylated on serine residues after ligand-receptor engagement. Forced expression of mLC7-1
induces specific TGF responses, including an activation of Jun
N-terminal kinase (JNK), a phosphorylation of c-Jun, and an inhibition
of cell growth. Furthermore, TGF induces the recruitment of mLC7-1
to the intermediate chain of dynein. A kinase-deficient form of TGF
RII prevents both mLC7-1 phosphorylation and interaction with the
dynein intermediate chain (DIC). This is the first demonstration of a
link between cytoplasmic dynein and a natural growth inhibitory cytokine. Furthermore, our results suggest that TGF pathway
components may use a motor protein light chain as a receptor for the
recruitment and transport of specific cargo along microtublules.
These authors contributed equally to this work.
Present address: Lexicon Genetics Inc., 8800 Technology Forest Place, The Woodlands, TX 77381-1160.
Corresponding author. E-mail address:
kmm15{at}psu.edu.
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