LIM domain recognition of a tyrosine-containing tight turn

• Published in: The Journal of biological chemistry Vol. 269; no. 40; pp. 25085 - 25090
• Main Authors: Wu, R Y, Gill, G N
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 07-10-1994
• Subjects: Amino Acid Sequence; Base Sequence; DNA-Binding Proteins; Endocytosis; Exons; Homeodomain Proteins; LIM-Homeodomain Proteins; Molecular Sequence Data; Nerve Tissue Proteins; Receptor, Insulin - chemistry; Receptor, Insulin - genetics; Transcription Factors; Tyrosine; Zinc - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(17)31502-8

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.