4.1N binding regions of inositol 1,4,5-trisphosphate receptor type 1
4.1N binding regions of inositol 1,4,5-trisphosphate receptor type 1
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DOI：
10.1016/j.bbrc.2006.02.010
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发表时间：
2006-04-07
影响因子：
3.1
通讯作者：
Mikoshiba, K
中科院分区：
文献类型：
--
作者：
Fukatsu, K;Bannai, H;Mikoshiba, K
张某等人。和马克西莫夫等人。[S.Zhang，A.Mizutani，C.Hisatsune，T.Higo，H.Bannai，T.Nakayama，M.Hattori，and K.Mikoshiba，Protein 4.1N是在极化的Madin-Darby犬肾细胞中将I型三磷酸肌醇受体转位到基侧膜域所需的蛋白4.1N，J.Biol。化学。278(2003)4048-4056；A.马克西莫夫，唐振山。和I.Bezprozvanny，I型肌醇(1，4，5)-三磷酸受体与神经元中4.1N蛋白的关联，Mol.牢房。神经科。22(2003)271-283。]报道了4.1N是肌醇1，4，5-三磷酸受体I型(IP(3)R1)的结合伙伴，但IP(3)R1的结合部位不同：前者确定细胞质尾部的C端14个氨基酸(CTT14aa)为结合部位。后者指定了另一个片段，细胞质尾部中部1(CTM1)。为了解决这一差异，我们进行了免疫沉淀，发现两个片段都具有与4.1N结合的活性。这两个片段也干扰了4.1N调节的IP3R1在神经元树突中的扩散。然而，缺乏CTT14aa的IP(3)R1(IP(3)R1-ACTT14aa)不与4.1N结合[S.Zhang，A.Mizutani，C.Hisatsune，T.Higo，H.Bannai，T.Nakayama，M.Hattori和K.Mikoshiba，Protein 4.In是肌醇1，4，5-三磷酸受体I型向基底外侧移位所必需的。极化的Madin-Darby犬肾细胞膜结构域，J.Biol。化学。2 78(2003)4048-4056。]其在神经元树突中的扩散常数大于IP(3)R1全长的扩散常数[K.Fukatsu，H.Bannai.张春生、中村、井上和三叶光一郎，肌醇1，4，5-三磷酸受体I型的横向扩散受肌动蛋白细丝和神经元树突中4.1N的调节，J.Biol。化学。第279(2004年)48976-48982.]结果表明，CTT14aa和CTM1序列均能以多肽形式与4.1N结合。然而，我们认为IP(3)R1全长四聚体形式的4.1N结合的负责结合部位是CTT14aa。(C)2006 Elsevier Inc.保留所有权利。
Zhang et al. and Maximov et al. [S. Zhang, A. Mizutani, C. Hisatsune, T. Higo, H. Bannai, T. Nakayama, M. Hattori, and K. Mikoshiba, Protein 4.1 N is required for translocation of inositol 1,4,5-trisphosphate receptor type I to the basolateral membrane domain in polarized Madin-Darby canine kidney cells, J. Biol. Chem. 278 (2003) 4048-4056; A. Maximov, T. S. Tang. and I. Bezprozvanny, Association of the type I inositol (1,4,5)-trisphosphate receptor with 4.1 N protein in neurons, Mol. Cell. Neurosci. 22 (2003) 271-283.] reported that 4. 1 N is a binding partner of inositol 1,4,5-trisphosphate receptor type I (IP(3)R1), however the binding site of IP(3)R1 differed: the former determined the C-terminal 14 amino acids of the cytoplasmic tail (CTT14aa) as the binding site.. while the latter assigned another segment, cytoplasmic tail middle 1 (CTM1). To solve this discrepancy, we performed immunoprecipitation and found that both the segments had binding activity to 4.1N. Both segments also interfered the 4.1N-regulated IP3R1 diffusion in neuronal dendrites. However, IP(3)R1 lacking the CTT14aa (IP(3)R1-ACTT14aa) does not bind to 4. 1 N [S. Zhang, A. Mizutani, C. Hisatsune, T. Higo, H. Bannai, T. Nakayama, M. Hattori, and K. Mikoshiba, Protein 4. IN is required for translocation of inositol 1,4,5-trisphosphate receptor type I to the basolateral. membrane domain in polarized Madin-Darby canine kidney cells, J. Biol. Chem. 2 78 (2003) 4048-4056.] and its diffusion constant is larger than that of IP(3)R1 full-length in neuronal dendrites [K. Fukatsu, H. Bannai.. S. Zhang, H. Nakamura, T. Inoue, and K. Mikoshiba, Lateral diffusion of inositol 1,4,5-trisphosphate receptor type I is regulated by actin filaments and 4. 1 N in neuronal dendrites, J. Biol. Chem. 279 (2004) 48976-48982.]. We conclude that both the CTT14aa and CTM1 sequences can bind to 4.1N in peptide fragment forms. However, we propose that the responsible binding site for 4.1 N binding in full-length tetramer form of IP(3)R1 is CTT14aa. (c) 2006 Elsevier Inc. All rights reserved.