Isolation of PSD-Zip45, a novel Homer/vesl family protein containing leucine zipper motifs, from rat brain

• Published in: FEBS letters 1998-10, Vol.437 (3), p.304-308
• Main Authors: Sun, Jie, Tadokoro, Satoko, Imanaka, Takanobu, D. Murakami, Seiko, Nakamura, Mako, Kashiwada, Kouji, Ko, Jiae, Nishida, Wataru, Sobue, Kenji
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Brain Chemistry; Carrier Proteins - chemistry; Carrier Proteins - genetics; Cloning, Molecular; Homer Scaffolding Proteins; Leucine zipper; Leucine Zippers - genetics; Metabotropic glutamate receptor; Molecular Sequence Data; Multigene Family; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - isolation & purification; Neuropeptides - chemistry; Neuropeptides - genetics; PDZ domain; Postsynaptic density; Rats; Rats, Sprague-Dawley; Receptor clustering; Sequence Homology, Amino Acid
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(98)01256-3

Using monoclonal antibody against the 45 kDa postsynaptic density protein, we isolated a novel isoform of Homer/vesl. The NH 2-terminal region containing a PDZ domain of this protein is identical to that of Homer/vesl, and the COOH-terminal region containing unique leucine zippers shows self-multimerization. We named this protein PSD-Zip45. In addition to specific binding of PSD-Zip45 mediated by a PDZ domain to the metabotropic glutamate receptors 1α or 5, the distribution of PSD-Zip45 transcripts is highly consistent with that of metabotropic glutamate receptor transcripts. The PSD-Zip45 is, therefore, the first candidate as receptor anchoring proteins containing leucine zipper motifs in the central nervous system.