A Proline Residue in the α-Helical Rod Domain of Type I Keratin 16 Destabilizes Keratin Heterotetramers*
A Proline Residue in the α-Helical Rod Domain of Type I Keratin 16 Destabilizes Keratin Heterotetramers*
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I 型角蛋白 16 的 α-螺旋杆结构域中的脯氨酸残基使角蛋白异四聚体不稳定*
DOI：
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发表时间：
1997
影响因子：
4.8
通讯作者：
P. Coulombe
中科院分区：
文献类型：
--
作者：
M. Wawersik;R. Paladini;Erick N. Noensie;P. Coulombe
I型角蛋白14（K14）和16（K16）在它们的组装性质和它们的表达模式上是不同的，尽管具有高度的序列同一性。了解K16的功能和调节是有意义的，因为它在复层上皮损伤后位于伤口边缘的角质形成细胞中具有强烈的诱导作用。我们先前报道，与K14相比，K16与作为II型角蛋白配对伴侣的K5或K6形成不稳定的异源四聚体（Paladini，R. D、高桥，K.，太棒了，N。美国，和Coulombe，P. A.等（1996）J. Cell Biol.132，381-397）。我们在这里显示，又一个相关的I型角蛋白，K17，形成稳定的异源四聚体与各种II型角蛋白，进一步强调K16的独特性质。在异源四聚体形成试验中对嵌合K14-K16蛋白的分析表明，不稳定性决定簇位于K16的α-螺旋杆结构域内的220个氨基酸片段中。定点突变显示，Pro 188，一个氨基酸残基位于亚结构域1B的杆，占定量的不稳定性K16-含有异源四聚体在变性条件下。体外聚合研究表明，Pro 188的存在与组装效率的降低相关。除了他们的影响角蛋白异四聚体的稳定构象，这些研究结果表明，K16的四聚体形成特性可能会影响其之间的分配的可溶性和聚合物池，因此有助于其调节上皮细胞在休息和伤口修复条件下。
The type I keratins 14 (K14) and 16 (K16) are distinct in their assembly properties and their expression pattern despite a high degree of sequence identity. Understanding K16 function and regulation is of interest, given its strong induction in keratinocytes located at the wound edge after injury to stratified epithelia. We reported previously that, compared with K14, K16 forms unstable heterotetramers with either K5 or K6 as the type II keratin pairing partner (Paladini, R. D., Takahashi, K., Bravo, N. S., and Coulombe, P. A. (1996) J. Cell Biol. 132, 381–397). We show here that yet another related type I keratin, K17, forms stable heterotetramers with a variety of type II keratins, further accentuating the unique nature of K16. Analysis of chimeric K14-K16 proteins in a heterotetramer formation assay indicated that the instability determinant resides in a 220-amino acid segment within the α-helical rod domain of K16. Site-directed mutagenesis revealed that Pro188, an amino acid residue located in subdomain 1B of the rod, accounts quantitatively for the instability of K16-containing heterotetramers under denaturing conditions. In vitropolymerization studies suggest that the presence of Pro188correlates with a reduction in assembly efficiency. In addition to their implications for the stable conformation of the keratin heterotetramers, these findings suggest that the tetramer-forming properties of K16 may influence its partitioning between the soluble and polymer pools, and hence contribute to its regulation in epithelial cells under resting and wound repair conditions.
杆域中的电荷相互作用驱动中间丝组装过程中四聚体的形成。
DOI：
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发表时间：
1994
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Meng,JJ;Khan,S;Ip,W
通讯作者：
Ip,W
“简单”上皮细胞中有显着的可溶性角蛋白部分。
影响因子：
4
作者：
Chou,CF;Riopel,CL;Rott,LS;Omary,MB
通讯作者：
Omary,MB
DOI：
10.1006/bbrc.1995.1051
发表时间：
1995-01-05
影响因子：
3.1
作者：
LOWTHERT, LA;KU, NO;OMARY, MB
通讯作者：
OMARY, MB