BAALC 1-6-8 protein is targeted to postsynaptic lipid rafts by its N-terminal myristoylation and palmitoylation, and interacts with alpha, but not beta, subunit of Ca2+/calmodulin-dependent protein kinase II

作者：Wang X; Tian QB; Okano A; Sakagami H; Moon IS; Kondo H; Endo S; Suzuki T^*

来源：Journal of Neurochemistry, 2005, 92(3): 647-659.

DOI：10.1111/j.1471-4159.2004.02902.x

• brain and acute leukemia cytoplasmic protein
• Ca2+
• calmodulin-dependent protein kinase II
• myristoylation
• palmitoylation
• postsynaptic density
• postsynaptic lipid raft

We cloned a rat BAALC 1-6-8 isoform cDNA (GenBank(TM) 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 alpha, but not beta, subunit of Ca2+/calmodulin-dependent protein kinase II (CaMKIIalpha). 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 CaMKIIalpha, which contains alpha isoform-specific sequence. Thus, the interaction may be CaMKIIalpha-specific. We also found that BAALC 1-6-8 protein, as well as CaMKIIalpha, 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 CaMKIIalpha.

• 出版日期2005-2
• 单位河北医科大学