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Vol. 10, Issue 6, 1973-1984, June 1999
-Tropomyosin
Department of Medicine, University of California at San Diego, La
Jolla, California 92093-0650
PDZ and LIM domains are modular protein interaction motifs present
in proteins with diverse functions. Enigma is representative of a
family of proteins composed of a series of conserved PDZ and LIM
domains. The LIM domains of Enigma and its most related family member,
Enigma homology protein, bind to protein kinases, whereas the PDZ
domains of Enigma and family member actin-associated LIM protein bind
to actin filaments. Enigma localizes to actin filaments in fibroblasts
via its PDZ domain, and actin-associated LIM protein binds to
and colocalizes with the actin-binding protein 
-actinin-2 at Z lines
in skeletal muscle. We show that Enigma is present at the Z line in
skeletal muscle and that the PDZ domain of Enigma binds to a skeletal
muscle target, the actin-binding protein tropomyosin (skeletal 
-TM).
The interaction between Enigma and skeletal -TM was specific for the
PDZ domain of Enigma, was abolished by mutations in the PDZ domain, and
required the PDZ-binding consensus sequence (Thr-Ser-Leu) at the
extreme carboxyl terminus of skeletal -TM. Enigma interacted with
isoforms of tropomyosin expressed in C2C12 myotubes and formed an
immunoprecipitable complex with skeletal -TM in transfected cells.
The association of Enigma with skeletal -TM suggests a role for
Enigma as an adapter protein that directs LIM-binding proteins to actin
filaments of muscle cells.
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