...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains.
【24h】

Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains.

机译：洞穴蛋白支架结构区和SRC的膜结合区形成侧向膜结构域。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Formation of domains by the membrane binding motifs of caveolin and src were studied in large unilamellar vesicles using fluorescence digital imaging microscopy. Caveolin, a major structural protein of caveolae, contains a scaffolding region (residues 82-101) that contributes to the binding of the protein to the plasma membrane. A caveolin peptide (82-101) corresponding to this scaffolding region induced the formation of membrane domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol-4,5-bisphosphate. Cholesterol, another predominant component of caveolae, was also enriched in these domains. Caveolae also contain many different signaling molecules including src family tyrosine kinases. Src proteins bind to the plasma membrane via a N-terminal myristate chain and a cluster of basic residues that can interact electrostatically with negatively charged lipids. A peptide corresponding to the src membrane binding motifs (residues myr-2-19) sequestered acidic lipids into lateral membrane domains. Both the src and the caveolin peptides colocalized together with acidic lipids in the domains. Control experiments show the domains are not the result of vesicle aggregation. Two-photon fluorescence correlation spectroscopy experiments suggest diffusion in the domains was slower, but the domains were dynamic. Protein kinase C phosphorylated src in its N-terminal membrane binding region; however, the caveolin scaffolding peptide inhibited this activity. Consequently, protein-induced membrane domains may affect cell signaling by organizing signal transduction components within the membrane and changing reaction rates.
机译：使用荧光数字成像显微镜研究了在大单层囊泡中由caveolin和src的膜结合基序形成的结构域。小窝蛋白是小窝蛋白的主要结构蛋白，其包含一个支架区域（残基82-101），有助于该蛋白与质膜的结合。对应于该支架区域的小窝蛋白肽（82-101）诱导形成富含酸性脂质磷脂酰丝氨酸和磷脂酰肌醇-4，5-双磷酸酯的膜结构域。海绵体的另一主要成分胆固醇也富集在这些区域中。 Caveolae还包含许多不同的信号分子，包括src家族的酪氨酸激酶。 Src蛋白通过N末端肉豆蔻酸酯链和可以与带负电的脂质发生静电相互作用的碱性残基簇与质膜结合。对应于src膜结合基序的肽（残基myr-2-19）将酸性脂质螯合到侧膜结构域中。 src和caveolin肽都与酸性脂质在域中共定位。对照实验表明，该域不是囊泡聚集的结果。两光子荧光相关光谱实验表明，在域中的扩散较慢，但域是动态的。蛋白激酶C在其N-末端膜结合区域中磷酸化了src;然而，小窝蛋白支架肽抑制了该活性。因此，蛋白质诱导的膜结构域可通过组织膜内的信号转导成分并改变反应速率来影响细胞信号传导。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号