Phosphorylation promotes the endonuclease-like activity of human centrin 2

Yang, Jing; Zhao, Yaqin; Yang, Binsheng

doi:10.1039/d2ra03402f

Cited by 2 publications

(1 citation statement)

References 56 publications

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“…Of note, another initially centrosomal protein is involved in the NER process: centrin 2 (human centrin 2, HsCen2, CEN2). In the nucleus, HsCen2 forms a stable XPC–RAD23B–CEN2 complex [ 164 ], influences the XPA–RPA binding to DNA [ 165 ], and even possesses an endonuclease-like activity [ 166 ].…”

Section: The Ways To Control Xpamentioning

confidence: 99%

The XPA Protein—Life under Precise Control

Krasikova

Lavrik

Rechkunova

2022

Cells

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Nucleotide excision repair (NER) is a central DNA repair pathway responsible for removing a wide variety of DNA-distorting lesions from the genome. The highly choreographed cascade of core NER reactions requires more than 30 polypeptides. The xeroderma pigmentosum group A (XPA) protein plays an essential role in the NER process. XPA interacts with almost all NER participants and organizes the correct NER repair complex. In the absence of XPA’s scaffolding function, no repair process occurs. In this review, we briefly summarize our current knowledge about the XPA protein structure and analyze the formation of contact with its protein partners during NER complex assembling. We focus on different ways of regulation of the XPA protein’s activity and expression and pay special attention to the network of post-translational modifications. We also discuss the data that is not in line with the currently accepted hypothesis about the functioning of the XPA protein.

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Section: The Ways To Control Xpamentioning

confidence: 99%

The XPA Protein—Life under Precise Control

Krasikova

Lavrik

Rechkunova

2022

Cells

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Interplay of Metal Ions and Posttranslational Modifications in Proteins

Peana,

Frączyk,

Zoroddu

2024

Eur J Inorg Chem

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Posttranslational modifications (PTMs) and metal ions are integral players in the complex regulatory orchestra governing protein function. Several metal ions, including zinc, iron, copper, and others, intricately influence protein structure and activity as cofactors. Concurrently, PTMs, such as phosphorylation, acetylation, and ubiquitination, add an additional layer of complexity to the proteome, dynamically shaping cellular responses. Understanding this bidirectional relationship is crucial for unraveling the complex web of cellular regulation. This review explores the reciprocal impact of metal ions on PTMs and vice versa and provides examples and insights into how metal ions modulate PTMs and, conversely, how PTMs influence metal‐binding proteins, shedding light on the complex crosstalk between these two crucial facets of cellular biology. This interplay is not only central to cellular homeostasis but also holds implications for diseases associated with dysregulated metal‐ion and PTM processes.

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Phosphorylation promotes the endonuclease-like activity of human centrin 2

Abstract: Phosphorylation weakened the binding of Tb3+ to HsCen2, enhanced the binding of DNA to HsCen2; and improves the endonuclease-like activity of HsCen2; Additionally, the endonuclease-like activity of HsCen2 or HsCen2p is regulated up by Tb3+-binding.

Cited by 2 publications

References 56 publications

The XPA Protein—Life under Precise Control

The XPA Protein—Life under Precise Control

Interplay of Metal Ions and Posttranslational Modifications in Proteins

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