Differential palmitoylation of two mouse glutamate receptor interacting protein 1 forms with different N-terminal sequences
| Autor: | Kanju Ikeno, Toshikazu Kakizaki, Kenji Sakimura, Masahiko Watanabe, Manabu Abe, Maya Yamazaki, Masahiro Fukaya |
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| Rok vydání: | 2001 |
| Předmět: |
Protein family
General Neuroscience Alternative splicing PDZ domain Palmitic Acid Glutamate receptor Nerve Tissue Proteins AMPA receptor Biology Mice Prosencephalon Animals Newborn Palmitoylation Biochemistry Cerebellum Complementary DNA COS Cells Animals RNA Splice Sites Receptors AMPA Enzyme Inhibitors Carrier Proteins Postsynaptic density Adaptor Proteins Signal Transducing Gene Library |
| Zdroj: | Neuroscience Letters. 304:81-84 |
| ISSN: | 0304-3940 |
| Popis: | Glutamate receptor interacting protein (GRIP) is a member of the PDZ domain-containing protein family that is localized in the postsynaptic density area. This protein has been reported to interact specifically with the C-termini of AMPA-selective glutamate receptor channel subunits, GluRα2 and GluRα3 through its PDZ domains. To clarify the physiological functions of GRIP, we cloned mouse GRIP1, and found that there are three sites for alternative splicing and two putative translational start codons by characterizing GRIP1 cDNA clones and reverse transcription-polymerase chain reaction products. Metabolic labeling of COS-7 cells expressing two N-terminal GRIP1 proteins demonstrated that these proteins differed in their pattern of palmitoylation. These findings suggested that the molecular diversity of GRIP1 underlies the localization and functional heterogeneity of this protein. |
| Databáze: | OpenAIRE |
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