LIM domain recognition of a tyrosine-containing tight turn.
Endocytosis of cell surface receptors requires sequence "codes" consisting of tight turn structures with an essential Tyr or Phe residue. To determine mechanisms through which cells recognize this information, we utilized exon 16 of the human insulin receptor in the two-hybrid system to isolate a novel 455-amino acid cytoplasmic protein that contains two LIM domains within its carboxyl terminus. Mutational analyses indicate that one of the Cys-rich Zn2+ binding LIM domains specifically recognizes active but not inactive endocytic codes contained in exon 16. These findings suggest that LIM domain structures in proteins provide molecular recognition of Tyr-containing tight turn structures.
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Department of Biology, University of California San Diego, La Jolla 92093-0650.
Gill
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D000595:Amino Acid Sequence; D001483:Base Sequence; D004268:DNA-Binding Proteins; D004705:Endocytosis; D005091:Exons; D018398:Homeodomain Proteins; D060850:LIM-Homeodomain Proteins; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins; D011972:Receptor, Insulin / Q000737:chemistry* / Q000235:genetics; D014157:Transcription Factors; D014443:Tyrosine; D015032:Zinc / Q000378:metabolism
D004268:DNA-Binding Proteins; D018398:Homeodomain Proteins; D060850:LIM-Homeodomain Proteins; D009419:Nerve Tissue Proteins; D014157:Transcription Factors; C063843:insulin gene enhancer binding protein Isl-1; D014443:Tyrosine; D011972:Receptor, Insulin; D015032:Zinc