Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
Phosphorylation01:02

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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Impact of White Noise Therapy on Knee Joint Function and Quality of Life in Patients with Meniscus Injuries.

Noise & health·2026
Same author

Chinese expert consensus: Radioactive iodine-125 seed interstitial brachytherapy for retroperitoneal lymph node metastases (2024 edition).

Journal of cancer research and therapeutics·2026
Same author

Hippo Signaling Suppresses Cell Ploidy and Tumorigenesis through Skp2.

Cancer cell·2026
Same author

Postoperative cytotoxic cerebral edema following surgical resection of a giant right atrial aneurysm in an infant: a rare case report.

Therapeutic advances in cardiovascular disease·2026
Same author

Identification and Spatial Differentiation of High-Risk Areas for Brown Bear Incidents in Yushu Prefecture, China, Using Machine Learning and Remote Sensing.

Animals : an open access journal from MDPI·2026
Same author

Transcriptome and metabolome analysis reveals that cuproptosis in bovine cumulus cells triggers the intercellular transmission of senescence and mitochondrial dysfunction to impair oocyte quality.

Theriogenology·2026

関連する実験動画

Updated: May 20, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

アセチル化依存によるSkp2機能の調節

Hiroyuki Inuzuka1, Daming Gao, Lydia W S Finley

  • 1Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.

Cell
|July 10, 2012
PubMed
まとめ

p300とSIRT3によって調節される異常なSkp2アセチル化は,Skp2の安定性を高め,がん細胞の移動と増殖を促進する. このアセチル化メカニズムは,Skp2を制御する.

さらに関連する動画

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

関連する実験動画

Last Updated: May 20, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

科学分野:

  • 分子腫瘍学 分子腫瘍学
  • エピジェネティクス エピジェネティクス
  • 癌生物学 癌生物学について

背景:

  • 異常なSkp2シグナル伝達は,腫瘍発生の重要な要因である.
  • サイトプラズミックSkp2は,攻撃的な乳がんや前立腺がんと相関しているが,そのメカニズムは不明である.

研究 の 目的:

  • Skp2.2のアセチル化依存調節を解明する.
  • 癌の進行における細胞質Skp2の役割を調査する.

主な方法:

  • P300によるSkp2アセチル化とSIRT3.3による脱アセチル化が調査されました.
  • Cdh1経路経由でSkp2の安定性とタンパク質分解を分析した.
  • 細胞増殖と腫瘍発生を評価するためにアセチル化模倣変異体を使用した.
  • Skp2の局所化,E-cadherinのユビキチン化,そして細胞の移動を調査した.

主要な成果:

  • Skp2は,K68とK71のp300によってアセチル化され,SIRT3.3によって敵対されます.
  • SIRT3の無活性化により,Skp2のアセチル化が増加し,Cdh1媒介による分解を抑制することで安定性が向上する.
  • アセチル化模倣型Skp2変異体は増殖と腫瘍発生が増加しています.
  • 核局所化信号 (NLS) のSkp2アセチル化は,細胞プラズマの保持を促進する.
  • サイトプラズミックSkp2は,E-カデリンのユビキチン化と分解を促すことで移住を促進します.

結論:

  • Skp2の腫瘍性機能に対する新しいアセチル化依存の規制メカニズムを特定しました.
  • 細胞プラズマのSkp2が,E-カデリン調節を通して細胞移動を制御することを実証した.
  • 攻撃的ながんにおけるSkp2の役割に関するメカニズム的洞察を提供します.