相关实验视频
Updated: Sep 19, 2025

09:16
Oligopeptide Competition Assay for Phosphorylation Site Determination
Published on: May 18, 2017
8.5K
解开蛋白激酶C-delta (PKC-δ) 的调节网络
Darshan Hebbal Raghu1, Leona Dcunha1, Mukhtar Ahmed2
1Centre for Integrative Omics Data Science (CIODS), Yenepoya (Deemed to be University), Mangalore, Karnataka 575018, India.
概括
这项研究确定了关键的PRKCD酸盐 (S302,S304),对于激酶活性和下游信号传输至关重要. 这些部位调节细胞循环,运动,粘附和迁移,为癌症进展提供了洞察力.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 蛋白激酶C Delta (PRKCD) 是一个关键激酶,参与关键的细胞过程,如DNA修复和致癌.
- 在各种生物状态下,PRKCD的酸化经常发生变化,正如在蛋白组学研究中观察到的.
研究的目的:
- 分析公开可用的蛋白组学数据,以确定PRKCD的关键调节网络.
- 确定特定的PRKCD酸盐对其酶活性和下游信号传导至关重要.
主要方法:
- 使用了大量数据集 (315个蛋白学研究) 来识别一致的过酸化PRKCD位点.
- 进行同差调节分析,将PRKCD酸盐与基质和激酶活性联系起来.
主要成果:
- 确定S302和S304为PRKCD主导的自酸化和激活部位,显示与基质的显著共同调节.
- 发现S302和S304与酶活性和下游基质调节的相关性比以前已知的网站 (Y313,Y334,Y374) 更强烈.
- 突出了Y313,Y334和Y374作为与压力信号和癌症进展相关的酸盐.
结论:
- PRKCD的S302和S304位点对于激酶激活至关重要,并在调节下游通路中发挥中心作用.
- 这些发现为分析蛋白质组数据提供了一个强大的框架,以了解PRKCD在细胞过程和疾病中的作用.
相关概念视频
Amplifying Signals via Enzymatic Cascade
9.9K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
9.9K
Protein Kinases and Phosphatases
13.5K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.5K
cAMP-dependent Protein Kinase Pathways
6.7K
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,...
6.7K
Calmodulin-dependent Signaling
5.3K
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,...
5.3K
IP3/DAG Signaling Pathway
12.5K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
12.5K
PI3K/mTOR/AKT Signaling Pathway
4.0K
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
4.0K

