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Related Concept Videos

Phosphorylation01:02

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.
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...
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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.
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The Proteasome01:13

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Protein Kinases and Phosphatases02:54

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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.
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Biosynthesis of Nucleic Acids01:28

Biosynthesis of Nucleic Acids

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Nucleic acid biosynthesis is a fundamental biochemical process that produces the purine and pyrimidine nucleotides essential for DNA and RNA synthesis. This pathway maintains a balanced nucleotide pool, preventing imbalances that could jeopardize genetic integrity and cellular function. Given the crucial role of nucleotides, their synthesis is tightly regulated to ensure proper cellular homeostasis.Purine BiosynthesisThe biosynthesis of purine nucleotides begins with ribose-5-phosphate, a...
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Sumoylation in Physiology, Pathology and Therapy.

Umut Sahin1, Hugues de Thé2,3,4, Valérie Lallemand-Breitenbach2,3

  • 1Center for Life Sciences and Technologies, Department of Molecular Biology and Genetics, Bogazici University, Istanbul 34342, Turkey.

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Summary

Sumoylation, a vital protein modification, regulates cellular functions, development, and stress responses. Aberrant sumoylation is linked to diseases like cancer, making it a potential therapeutic target.

Keywords:
cancerinfectionneurodegenerationpost-translational modificationsmall ubiquitin-like modifierstressubiquitin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Sumoylation is a crucial post-translational modification regulating protein function, stability, and localization in eukaryotic cells.
  • It plays key roles in transcription, nuclear integrity, cell proliferation, senescence, lineage commitment, stemness, and epigenetic processes.
  • Sumoylation is also involved in infection, immune responses, and organismal development.

Purpose of the Study:

  • To review the multifaceted roles of sumoylation in cellular and physiological processes.
  • To highlight the involvement of sumoylation in various pathological conditions, including cancer and neurodegeneration.
  • To discuss the potential of sumoylation as a novel drug target in translational medicine.

Main Methods:

  • This review synthesizes existing literature on sumoylation.
  • It examines the regulatory functions of sumoylation across different biological contexts.
  • The review discusses the link between dysregulated sumoylation and disease pathogenesis.

Main Results:

  • Sumoylation modulates thousands of target substrates, influencing protein interactions and cellular functions.
  • It is critical for development and orchestrating responses to environmental stresses like hypoxia and nutrient deprivation.
  • Aberrant sumoylation is associated with cancer, neurodegeneration, and other diseases, while therapeutic modulation shows promise, as seen in acute promyelocytic leukemia (APL).

Conclusions:

  • Sumoylation is a fundamental regulatory mechanism with broad implications in health and disease.
  • Dysregulation of sumoylation contributes to various pathologies, underscoring its clinical relevance.
  • Sumoylation represents a promising, albeit complex, target for therapeutic intervention in translational medicine.