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BAALC 1‐6‐8 protein is targeted to postsynaptic lipid rafts by its N‐terminal myristoylation and palmitoylation, and interacts with α, but not β, subunit of Ca 2+ /calmodulin‐dependent protein kinase II
Author(s) -
Wang Xin,
Tian QingBao,
Okano Akira,
Sakagami Hiroyuki,
Moon Il Soo,
Kondo Hisatake,
Endo Shogo,
Suzuki Tatsuo
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2004.02902.x
Subject(s) - postsynaptic density , palmitoylation , myristoylation , biology , gene isoform , protein subunit , microbiology and biotechnology , postsynaptic potential , lipid raft , biochemistry , phosphorylation , signal transduction , receptor , cysteine , gene , enzyme
We cloned a rat BAALC 1‐6‐8 isoform cDNA (GenBank™ Accession No. AB073318 ) that encoded a 22‐kDa protein, and identified endogenous BAALC 1‐6‐8 protein in the brain. The gene was expressed widely in the frontal part of the brain, and the protein was localized to the synaptic sites and was increased in parallel with synaptogenesis. The protein interacted with the α, but not β, subunit of Ca 2+ /calmodulin‐dependent protein kinase II (CaMKIIα). The interaction occurred between the N‐terminal 35‐amino‐acid region of BAALC 1‐6‐8 protein and the C‐terminal end of the regulatory domain of CaMKIIα, which contains α isoform‐specific sequence. Thus, the interaction may be CaMKIIα‐specific. We also found that BAALC 1‐6‐8 protein, as well as CaMKIIα, was localized to lipid rafts and that both myristoylation and palmitoylation of BAALC 1‐6‐8 N‐terminal portion were required for targeting of the protein into lipid rafts. These findings suggest that BAALC 1‐6‐8 protein play a synaptic role at the postsynaptic lipid raft possibly through interaction with CaMKIIα.