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      Elfin is expressed during early heart development.

      Journal of Cellular Biochemistry
      Actinin, metabolism, Amino Acid Sequence, Animals, Cell Line, Cytoplasm, Cytoskeleton, DNA, Complementary, Gene Expression Regulation, Developmental, Green Fluorescent Proteins, Heart, embryology, In Situ Hybridization, LIM Domain Proteins, Luminescent Proteins, Mice, Molecular Sequence Data, Myocardium, Protein Binding, Protein Structure, Tertiary, RNA, Messenger, Sequence Homology, Amino Acid, Stress Fibers, Time Factors, Tissue Distribution, Transcription Factors, biosynthesis, chemistry

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          Abstract

          Elfin (previously named CLIM1) is a protein that possesses an N-terminal PDZ domain and a C-terminal LIM domain. It belongs to the family of Enigma proteins. Enigma proteins are a family of cytoplasmic proteins that contain an N-terminal PDZ domain and a series of C-terminal LIM domains. By virtue of these two protein interacting domains, Enigma proteins are capable of protein-protein interactions. It has been proposed that Enigma proteins may act as adapters between kinases and the cytoskeleton. We have previously shown that Elfin is most abundantly expressed in the heart and it colocalizes with alpha-actinin 2 at the Z-disks of the myocardium. In this report, Elfin was shown to localize at the actin stress fibers of myoblasts, as revealed by green fluorescent protein (GFP) tagging. In situ hybridization and immunostaining showed that Elfin expression begins at an early stage in mouse development and is present throughout the developing heart. Taken together, our experimental results suggest that Elfin may play an important role in myofibrillogenesis and heart development. Copyright 2001 Wiley-Liss, Inc.

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