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Related Concept Videos

Small GTPases - Ras and Rho01:24

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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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Related Experiment Video

Updated: Feb 14, 2026

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

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RAS GTPases are modified by SUMOylation.

Byeong Hyeok Choi1, Changyan Chen2, Mark Philips3

  • 1Department of Environmental Medicine, New York University Langone Medical Center, New York, NY, USA.

Oncotarget
|February 14, 2018
PubMed
Summary
This summary is machine-generated.

RAS proteins, crucial for cell signaling, are modified by SUMOylation. This new posttranslational modification, involving SUMO3, affects RAS protein activity and may control its function in cellular processes.

Keywords:
RASoncogenesispost-translational modificationsumoylation

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • RAS proteins are GTPases regulating vital cellular processes like survival and proliferation.
  • RAS mutations drive oncogenic transformation and tumorigenesis.
  • The small ubiquitin-related modifier (SUMO) pathway controls protein stability, activity, and localization.

Purpose of the Study:

  • To investigate if RAS proteins undergo SUMOylation.
  • To identify the specific SUMO isoform involved.
  • To explore the functional implications of RAS SUMOylation.

Main Methods:

  • Western blotting to detect SUMOylation.
  • Site-directed mutagenesis to identify SUMOylation sites.
  • Co-immunoprecipitation to study protein interactions.
  • Enzyme assays to assess deSUMOylation.

Main Results:

  • All three RAS isoforms (HRAS, KRAS, NRAS) are modified by SUMO3.
  • KRAS SUMOylation is observed in various cell lines.
  • SUMOylation is reversible, mediated by SENP1 and SENP2.
  • Lysine-42 is a key SUMOylation site.
  • PIASγ interacts with RAS and promotes its SUMOylation.
  • RAS SUMOylation is associated with RAS activation.

Conclusions:

  • RAS proteins are subject to SUMOylation, a novel posttranslational modification.
  • SUMOylation by SUMO3, regulated by PIASγ, affects RAS activity.
  • This modification may serve as a regulatory mechanism for RAS function.