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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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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Rap1 activity and localization is regulated by Rab40/CRL5 facilitated mono-ubiquitylation.

Andrew Neumann1, Revathi Sampath1, Ke-Jun Han1

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Rab40/CRL5 E3 ubiquitin ligase complex mono-ubiquitylates Rap1, a GTPase crucial for cell migration. This modification is essential for Rap1

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Rap GTPases regulate actin dynamics and cell migration.
  • Mechanisms of Rap GTPase activation and localization are not fully understood.
  • Rab40/CRL5-dependent mono-ubiquitylation regulates Rap2 activation.

Purpose of the Study:

  • To investigate the role of mono-ubiquitylation in Rap1 regulation.
  • To determine if Rab40/CRL5 targets Rap1 for ubiquitylation.
  • To elucidate the impact of Rap1 mono-ubiquitylation on its localization and activity.

Main Methods:

  • Ubiquitylation assays
  • Immunoprecipitation
  • Confocal microscopy
  • Western blotting

Main Results:

  • Rap1 undergoes mono-ubiquitylation mediated by a Rab40/CRL5 E3 ubiquitin ligase complex.
  • Rap1 mono-ubiquitylation is essential for its proper localization to the plasma membrane and nuclear envelope.
  • This finding extends the role of Rab40/CRL5 to the regulation of Rap1 activity and dynamics.

Conclusions:

  • Rab40/CRL5 is a key regulator of Rap GTPase family members, including Rap1.
  • Mono-ubiquitylation by Rab40/CRL5 controls Rap1's spatiotemporal dynamics and subcellular localization.
  • This study provides novel insights into the post-translational regulation of Rap GTPases.