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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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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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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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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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Dual Specificity Phosphatase 5-Substrate Interaction: A Mechanistic Perspective.

Raman G Kutty1, Marat R Talipov2, Robert D Bongard3

  • 1Department of Pediatrics, Division of Neonatology, Department of Obstetrics and Gynecology, Developmental Vascular Biology Program, Translational and Biomedical Research Center, Milwaukee, Wisconsin, USA.

Comprehensive Physiology
|September 16, 2017
PubMed
Summary
This summary is machine-generated.

Dual Specificity Phosphatase 5 (DUSP5) is a key enzyme in cellular signaling. Molecular modeling reveals its specific interaction with phospho-extracellular signal-regulated kinase, offering insights into kinase signaling pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Mammalian genomes encode ~200 phosphatases that dephosphorylate proteins.
  • Dual Specificity Phosphatases (DUSPs) remove phosphate groups from serine/threonine and tyrosine residues.
  • DUSP5 is a member of the DUSP family with a specific role in cellular signaling.

Purpose of the Study:

  • To review the structure and function of Dual Specificity Phosphatase 5 (DUSP5).
  • To elucidate the mechanistic interaction and specificity of DUSP5 toward its substrate, phospho-extracellular signal-regulated kinase (p-ERK).
  • To discuss implications for mitogen-activated protein kinase (MAPK) signaling and phosphatase-targeted drug discovery.

Main Methods:

  • Comparative structural analysis of DUSP5 and other DUSPs.
  • Molecular modeling studies to investigate DUSP5-p-ERK interactions.
  • Review of small molecule inhibitor development targeting DUSP5.

Main Results:

  • DUSP5 exhibits unique structural features compared to other DUSPs.
  • Molecular modeling provides mechanistic insights into DUSP5's specificity for p-ERK.
  • New understanding of MAPK signaling pathways influenced by DUSP5's action.

Conclusions:

  • DUSP5's specific interaction with p-ERK is mechanistically explained.
  • Findings advance the understanding of MAPK signaling.
  • Lessons from DUSP5 targeting may guide efforts for other phosphatases.