関連する実験動画
Updated: Jul 13, 2026

11:13
Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
タイロシンリン酸化は,pp60c-srcの生化学的および生物学的性質を調節する
Cell
|April 10, 1987
まとめ
pp60c-srcにおけるチロシンリン酸化を調査すると,Tyr 527における低リン酸化とTyr 416における高リン酸化が,その完全な変換の可能性にとって極めて重要であることが明らかになる.
科学分野:
- 分子生物学は分子生物学である.
- 細胞生物学 細胞生物学
- バイオケミストリー バイオケミストリー
背景:
- pp60c-srcは原発性腫瘍型チロシンキナーゼである.
- タイロシンリン酸化は,キナーゼ活性と細胞変換の調節に重要な役割を果たします.
- 特定のチロシン残留物 (416,519,527) は,重要な規制領域である.
研究 の 目的:
- pp60c-src調節における特定のチロシンリン酸化部位の役割を明らかにする.
- Tyr 416,519,および527の改変がpp60c-srcの活性と細胞変異にどのように影響するか判断する.
主な方法:
- サイト指向型変異は,ppp60c-srcの416位,519位,527位のチロシンにフェニララニンを置換するために使用されました.
- 形態学的変容,柔らかいアガー成長,焦点形成の測定を行った.
- 変異したpp60c-srcタンパク質で,インビトロキナーゼ活性アッセイが行われました.
主要な成果:
- Tyr 527 (単独またはTyr 519と併用) を改変した突然変異者は,形態学的変異,軟アガーの成長,および焦点形成を示した.
- これらの変異体はまた,インビトロキナーゼ活性が上昇したことを示した.
- Tyr 416での置換はキナーゼ活性を部分的に抑制したが,Tyr 527の改変の文脈で変異フェノタイプを廃止した.
結論:
- pp60c-srcの完全な変換の可能性は,Tyr 527での低酸化を必要とします.
- Tyr 416における高酸化は,焦点形成および軟アガーの成長を誘発するために不可欠です.
- Tyr 527とTyr 416の両方のリン酸化状態は,pp60c-src媒介の細胞変容に不可欠である.
関連する概念動画
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...
Protein Kinases and Phosphatases
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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
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These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
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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 the...
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Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...

