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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Protein Kinases and Phosphatases02:54

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Phosphorylation01:02

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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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Amplifying Signals via Enzymatic Cascade01:22

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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...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Androgen receptor phosphorylation: biological context and functional consequences.

Yulia Koryakina1, Huy Q Ta1, Daniel Gioeli2

  • 1Department of MicrobiologyImmunology, and Cancer BiologyUVA Cancer CenterUniversity of Virginia, PO Box 800734, Charlottesville, Virginia 22908, USA.

Endocrine-Related Cancer
|January 16, 2014
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Androgen receptor (AR) phosphorylation by kinases is crucial for its function in diseases like prostate cancer. Understanding these modifications can lead to better AR-targeted therapies.

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Cancer Biology

Background:

  • The androgen receptor (AR) is a nuclear receptor regulating gene transcription.
  • AR signaling is vital in diseases such as prostate and breast cancer.
  • Current AR-targeted therapies face limitations due to restored AR signaling in advanced disease.

Purpose of the Study:

  • To review AR phosphorylation sites, responsible kinases, and their functional consequences.
  • To explore the biological context of AR post-translational modifications.
  • To discuss AR phosphorylation in clinical samples.

Main Methods:

  • Literature review of AR phosphorylation.
  • Analysis of kinase-mediated AR modifications.
  • Discussion of functional outcomes and clinical relevance.

Main Results:

  • AR is regulated by phosphorylation on serine, threonine, and tyrosine residues.
  • Specific kinases mediate these phosphorylations, impacting AR function.
  • AR phosphorylation patterns in clinical samples are partially understood.

Conclusions:

  • Understanding AR phosphorylation is key to developing improved therapeutics for AR-dependent diseases.
  • Targeting AR phosphorylation may overcome resistance to current therapies.
  • Further research into AR phosphorylation in clinical settings is warranted.