通过MAP激酶介导的c-jun的酸化
B J Pulverer1, J M Kyriakis, J Avruch
1Ludwig Institute for Cancer Research, London, UK.
Nature
|October 17, 1991
概括
这项研究表明,基因激活蛋白 (MAP) 激酶在c-jun蛋白上化特定部位,增强其活性. 这种酸化机制解释了各种生长信号如何激活c-jun转录因子.
科学领域:
- 分子生物学分子生物学
- 细胞信号传递 细胞信号传递
- 瘤发生的发生因子.
背景情况:
- 原始瘤基因c-jun是一种调节核事件的转录因子.
- c-jun活动是通过酸化调节的,特别是在carboxy终端的脱酸化.
- 细胞外刺激,包括醇,影响c-jun活动.
研究的目的:
- 通过mitogens调节的c-jun上确定特定的酸化点.
- 为了研究基激活蛋白 (MAP) 激酶在c-jun酸化中的作用.
- 为了确定MAP激酶介导的酸化如何影响c-jun的转录活性.
主要方法:
- 对c-jun的酸化位点进行测绘.
- 使用纯化的MAP激酶 (pp54,pp42/44) 的体外激酶试验.
- 在酸化后对c-jun交换活化活动的分析.
主要成果:
- 在c-jun氨基末端A1域中的两个氨酸残留物被确定为酸化的标.
- 中原体,醇和激活的ras在这些部位诱导酸化.
- MAP 激酶 pp54 和 pp42/44 特别酸化这些血清残留物,导致 c-jun 交换活化增加.
结论:
- 在A1域中,MAP激酶介导的特定氨酸残留物酸化积极调节c-jun活动.
- 这种机制提供了洞察力,让我们了解原体,生长因子和瘤基因通常是如何刺激c-jun的.
- 这些发现突出了细胞对生长信号反应的关键调节途径.
相关概念视频
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Microtubule Associated Proteins (MAPs)
Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
MAPK Signaling Cascades
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
cAMP-dependent Protein Kinase Pathways
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...


