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A more recent version of this article appeared on December 1, 2002
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Submitted on May 1, 2002
Revised on August 23, 2002
Accepted on August 23, 2002
1 Department of Pharmacology, Pennsylvania State University
College of Medicine, 500 University Dr., Hershey, PA 17033 (present address: Lexicon Genetics Inc., 8800 Technology Forest Place, The
Woodlands, TX 77381-1160)
2 Department of Pharmacology, Pennsylvania State University
College of Medicine, 500 University Dr., Hershey, PA 17033
* Corresponding author. E-mail address: kmm15{at}psu.edu.
The phosphorylated, activated cytoplasmic domains of the TGFß receptors were used as probes to screen an expression library that was prepared from a highly TGFß-responsive intestinal epithelial cell line. One of the TGFß receptor-interacting proteins isolated was identified to be the mammalian homologue of the LC7 family (mLC7) of dynein light chains (DLCs). This 11-kD cytoplasmic protein interacts with the TGFß receptor complex intracellularly and is phosphorylated on serine residues after ligand-receptor engagement. Forced expression of mLC7-1 induces specific TGFß responses, including an activation of JNK, a phosphorylation of c-Jun, and an inhibition of cell growth. Further, TGFß induces the recruitment of mLC7-1 to the intermediate chain of dynein (DIC). A kinase-deficient form of TGFß RII prevents both mLC7-1 phosphorylation and interaction with DIC. This is the first demonstration of a link between cytoplasmic dynein and a natural growth inhibitory cytokine. Further, our results suggest that TGFß pathway components may utilize a motor protein light chain as a receptor for the recruitment and transport of specific cargo along MTs.
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