Abstract：
: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, GluRalpha2 and GluRalpha3 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.
journal_name
Neurosci Lettjournal_title
Neuroscience lettersauthors
Yamazaki M,Fukaya M,Abe M,Ikeno K,Kakizaki T,Watanabe M,Sakimura Kdoi
10.1016/s0304-3940(01)01766-9keywords:
subject
Has Abstractpub_date
2001-05-18 00:00:00pages
81-4issue
1-2eissn
0304-3940issn
1872-7972pii
S0304394001017669journal_volume
304pub_type
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