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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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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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Phosphorylation01:02

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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.
These groups modify specific amino acids in a protein....
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

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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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Related Experiment Video

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Identification of Post-translational Modifications of Plant Protein Complexes
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Identification of Post-translational Modifications of Plant Protein Complexes

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Phytophthora infestans specific phosphorylation patterns and new putative control targets.

Itziar Frades1, Erik Andreasson1

  • 1Department of Plant Protection Biology, Swedish University of Agricultural Sciences, Alnarp, SE-230 53, Sweden.

Fungal Biology
|March 30, 2016
PubMed
Summary
This summary is machine-generated.

This study identifies novel gene targets in Phytophthora infestans by analyzing phosphorylation and small RNA regulation. These findings offer new strategies for developing pesticides and biological control agents against this oomycete pathogen.

Keywords:
CrinklersDiscriminative n-gramsPesticide targetsPhosphoproteomicssmall RNA

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Identification of Post-translational Modifications of Plant Protein Complexes
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Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Area of Science:

  • Molecular Biology
  • Computational Biology
  • Plant Pathology

Background:

  • Oomycetes, like Phytophthora infestans, pose significant threats to agriculture.
  • Understanding oomycete gene regulation is crucial for developing effective control strategies.
  • Existing control methods require new targets to combat resistance and improve efficacy.

Purpose of the Study:

  • To apply biomathematical searches to oomycete gene regulatory mechanisms.
  • To identify new potential targets for pesticides or biological control against Phytophthora infestans.
  • To investigate dual regulation by small RNA and phosphorylation in P. infestans.

Main Methods:

  • Discriminative n-gram analysis to identify oomycete phylum-specific phosphorylation motifs.
  • Biomathematical searches for gene regulatory mechanisms.
  • Second screen to identify proteins dually regulated by small RNA and phosphorylation.
  • Analysis of unique P. infestans proteins, including RxLR effectors, Crinkler (CRN) proteins, and elicitins.

Main Results:

  • Identified 11,600 P. infestans specific n-grams, mapping 642 phosphoproteins, predominantly involved in phosphatidylinositol metabolism.
  • Found 164 proteins dually regulated by small RNA and phosphorylation, with key roles in phosphatidylinositol signaling, endocytosis, and autophagy.
  • Identified specific phospho-motifs in CRN proteins across all life stages, with three CRN proteins (PITG_12626, PITG_14042, PITG_23175) showing species-specific phosphorylation and dual regulation.

Conclusions:

  • Biomathematical analysis reveals key regulatory mechanisms in P. infestans.
  • Phosphorylation and small RNA dual regulation highlight essential proteins for potential intervention.
  • CRN proteins with species-specific motifs represent promising targets for novel control strategies against Phytophthora infestans.