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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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A schema is a mental construct consisting of a cluster or collection of related concepts (Bartlett, 1932). There are many different types of schemata, and they all have one thing in common: schemata are a method of organizing information that allows the brain to work more efficiently. When a schema is activated, the brain makes immediate assumptions about the person or object being observed.
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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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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

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LRRK2 Phosphorylation: Behind the Scenes.

Tina De Wit1, Veerle Baekelandt1, Evy Lobbestael1

  • 11 Laboratory for Neurobiology and Gene Therapy, Department of Neurosciences, KU Leuven, Leuven, Belgium.

The Neuroscientist : a Review Journal Bringing Neurobiology, Neurology and Psychiatry
|February 2, 2018
PubMed
Summary
This summary is machine-generated.

Mutations in leucine-rich repeat kinase 2 (LRRK2) cause Parkinson's disease (PD). This review explores LRRK2 phosphorylation regulation and its impact on PD, including therapeutic strategies.

Keywords:
LRRK2Parkinson’s diseasekinase inhibitionphosphorylation

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Assaying the Kinase Activity of LRRK2 in vitro
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Assaying the Kinase Activity of LRRK2 in vitro
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Assaying the Kinase Activity of LRRK2 in vitro

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common genetic cause of Parkinson's disease (PD).
  • LRRK2 is a large protein with kinase and GTPase activity, acting as a scaffold in signaling pathways.
  • LRRK2 phosphorylation is crucial for its function, but its regulation and impact on PD are not fully understood.

Purpose of the Study:

  • To review the regulation of LRRK2 phosphorylation.
  • To explore the relationship between LRRK2 phosphorylation and its molecular/cellular functions in PD.
  • To discuss the implications of LRRK2 phosphorylation for therapeutic strategies.

Main Methods:

  • Literature review of studies on LRRK2 phosphorylation.
  • Analysis of LRRK2 structure, domains, and activities.
  • Examination of phosphorylation patterns in pathogenic LRRK2 mutants and in response to kinase inhibitors.

Main Results:

  • Pathogenic LRRK2 mutants show altered phosphorylation patterns, with increased autophosphorylation and decreased site-specific phosphorylation.
  • LRRK2 kinase inhibition affects phosphorylation sites similarly to pathogenic variants and can induce protein degradation.
  • Inhibitor-induced LRRK2 degradation may be linked to adverse effects, mimicking pathology in LRRK2 knockout models.

Conclusions:

  • LRRK2 phosphorylation is a complex regulatory mechanism with significant implications for Parkinson's disease.
  • Understanding LRRK2 phosphorylation is key to developing effective disease-modifying therapies for PD.
  • Further research into LRRK2 phosphorylation dynamics is essential for elucidating its role in PD pathogenesis and treatment.