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Covalently Linked Protein Regulators

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-ATCase

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 Complex

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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...

Phosphorylation

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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.
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Regulation of Nuclear Protein Sorting

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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 Reactions

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

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Regulación dependiente de la acetilación de la función Skp2

Hiroyuki Inuzuka¹, Daming Gao, Lydia W S Finley

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

|July 10, 2012

Resumen

La acetilación aberrante de Skp2, regulada por p300 y SIRT3, aumenta la estabilidad de Skp2 y promueve la migración y la proliferación de las células cancerosas. Este mecanismo de acetilación gobierna el Skp2.

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Área de la Ciencia:

Oncología Molecular Oncología Molecular
La epigenética es la epigenética.
Biología del cáncer Biología del cáncer.

Sus antecedentes:

La señalización aberrante de Skp2 es un factor clave en la tumorigénesis.
El Skp2 citoplasmático se correlaciona con cánceres de mama y próstata agresivos, pero los mecanismos no están claros.

Objetivo del estudio:

Para aclarar la regulación dependiente de la acetilación de Skp2.
Investigar el papel del Skp2 citoplasmático en la progresión del cáncer.

Principales métodos:

Se investigó la acetilación de Skp2 por p300 y la desacetilación por SIRT3.3.
Se analizó la estabilidad de Skp2 y la proteólisis a través de la vía Cdh1.
Utilizó mutantes acetilación-miméticos para evaluar la proliferación celular y la tumorigénesis.
Se examinó la localización de Skp2, la ubiquitinación de E-cadherina y la migración celular.

Principales resultados:

Skp2 es acetilado por p300 en K68 y K71, antagonizado por SIRT3.
La inactivación de SIRT3 aumenta la acetilación de Skp2, mejorando la estabilidad al inhibir la degradación mediada por Cdh1.
Los mutantes Skp2 que imitan la acetilación muestran un aumento de la proliferación y la tumorigénesis.
La acetilación de Skp2 en la señal de localización nuclear (NLS) promueve la retención citoplasmática.
El Skp2 citoplasmático mejora la migración promoviendo la ubiquitinación y degradación de la E-cadherina.

Conclusiones:

Se identificó un nuevo mecanismo regulador dependiente de la acetilación para la función oncogénica de Skp2.
Se demostró que el Skp2 citoplasmático controla la migración celular a través de la regulación de la E-caderina.
Proporciona una visión mecanicista del papel de Skp2 en los cánceres agresivos.