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Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
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GTPases and their Regulation02:14

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GTPases and their Regulation02:14

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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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GPCRs Regulate Adenylyl Cylase Activity01:09

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Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Assaying the Kinase Activity of LRRK2 in vitro
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L'RRK de Triomphe: a solution for LRRK2 GTPase activity?

Jonathon Nixon-Abell1,2, Daniel C Berwick3, Kirsten Harvey1

  • 1Department of Pharmacology, UCL School of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, U.K.

Biochemical Society Transactions
|December 4, 2016
PubMed
Summary

Leucine-rich repeat kinase 2 (LRRK2) is key in Parkinson's disease (PD) pathogenesis. Pathogenic mutations may cause PD by increasing LRRK2 GTPase activity, with a protective variant aiding research.

Keywords:
GTPasesParkinson's diseaseWnt proteinsleucine-rich repeat kinaseneurodegeneration

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Leucine-rich repeat kinase 2 (LRRK2) is implicated in Parkinson's disease (PD) pathogenesis.
  • The precise function of LRRK2 and the impact of mutations remain unclear.
  • LRRK2 mutations are a significant genetic factor in PD.

Purpose of the Study:

  • To elucidate the function of LRRK2, particularly its GTPase activity.
  • To understand how pathogenic mutations affect LRRK2 function in PD.
  • To investigate the role of the R1398H variant in LRRK2 function.

Main Methods:

  • Analysis of LRRK2 GTPase activity in relation to pathogenic mutations.
  • Investigating the effect of mutations in the Ras and Roc domains.
  • Characterization of the protective R1398H variant.

Main Results:

  • A consensus is emerging regarding the effect of pathogenic mutations on LRRK2 GTPase activity.
  • GTP-bound LRRK2 is identified as pathogenic.
  • LRRK2 functions as a GTPase activated by dimerisation.
  • The R1398H variant serves as a control for pathogenic mutations.

Conclusions:

  • LRRK2 GTPase activity is central to its role in PD.
  • Understanding LRRK2 function is crucial for developing PD treatments.
  • The R1398H variant provides a valuable tool for LRRK2 research.