New function of calreticulin: calreticulin-dependent mRNA destabilization.
New function of calreticulin: calreticulin-dependent mRNA destabilization.
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DOI：
10.1161/01.res.0000193564.46466.2a
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发表时间：
2005-11
影响因子：
20.1
通讯作者：
M. Yokoyama;K. Hirata
中科院分区：
文献类型：
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作者：
M. Yokoyama;K. Hirata
钙网蛋白于1974年首次被鉴定为肌肌浆网Ca2+结合蛋白，并于1989年分离出编码该蛋白的DNA。钙网蛋白是一种普遍存在的蛋白，存在于广泛的物种和所有有核细胞类型中，具有多种重要的生物学功能。人类钙钙蛋白基因包含9个外显子和8个内含子。推导的氨基酸序列表明，钙网蛋白在其N端有17个氨基酸的疏水信号序列，成熟的钙网蛋白含有400个氨基酸。钙网蛋白的结构已被很好地表征它至少有3个结构域和功能域（图）。钙网蛋白的结构。该图显示了钙网蛋白结构域的基因组结构示意图。钙调蛋白的结构预测表明，该蛋白至少有3个结构域和功能域。编码钙网蛋白N结构域（包括N端信号序列）、P结构域和C结构域的外显子分别为蓝色、红色和绿色。N， P和C结构域也以蓝色，红色和绿色表示。该蛋白包含一个n端氨基酸信号序列（黑色框）和一个c端KDEL ER检索信号。指出了钙钙蛋白N结构域的3个半胱氨酸残基和二硫桥的位置。箭头表示潜在糖基化位点的位置（残基162和327）。重复A（氨基酸序列PXXIXDPDAXKPEDWDE）…
See related article, pages 1001–1008 Calreticulin was first identified as a Ca2+-binding protein of the muscle sarcoplasmic reticulum in 1974, and the DNA encoding this protein was isolated in 1989.1 Calreticulin is a ubiquitous protein, found in a wide range of species and in all nucleated cell types, and has a variety of important biological functions. The human gene for calreticulin contains 9 exons and 8 introns. The deduced amino acid sequence indicates that calreticulin has a 17 amino acid hydrophobic signal sequence at its N terminus and that mature calreticulin contains 400 amino acids. The structure of calreticulin has been well characterized.2 It has at least 3 structural and functional domains (Figure). Structure of calreticulin protein. The Figure shows a schematic representation of the genomic configuration of domain structure of calreticulin protein. Structural predictions for calreticulin suggest that the protein has at least 3 structural and functional domains. Exons encoding the N domain (including the N-terminal signal sequence), the P domain, and the C domain of calreticulin are in blue, red, and green respectively. The N, P, and C domains are also presented in blue, red, and green. The protein contains an N-terminal amino acid signal sequence (black box) and a C-terminal KDEL ER retrieval signal. The locations of 3 cysteine residues and the disulphide bridge in the N domain of calreticulin are indicated. The arrowheads indicate the location of potential glycosylation sites (residues 162 and 327). Repeats A (amino acid sequence PXXIXDPDAXKPEDWDE) …