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Related Concept Videos

Rab Proteins01:14

Rab Proteins

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.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
The Eukaryotic Promoter Region02:40

The Eukaryotic Promoter Region

The eukaryotic promoter region is a segment of DNA located upstream of a gene. It contains an RNA polymerase binding site, a transcription start site, and several cis-regulatory sequences.  The proximal promoter region is located in the vicinity of the gene and has cis-regulatory sequences and the core promoter. The core promoter is the binding site for RNA polymerase and is usually located between -35 and +35 nucleotides from the transcription start site. The distal promoter regions are...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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:
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...

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Updated: May 10, 2026

Using SCOPE to Identify Potential Regulatory Motifs in Coregulated Genes
07:55

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Published on: May 31, 2011

Defining the RGG/RG motif.

Palaniraja Thandapani1, Timothy R O'Connor, Timothy L Bailey

  • 1Terry Fox Molecular Oncology Group and Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research and Departments of Oncology and Medicine, McGill University, Montreal, Quebec H3T 1E2, Canada.

Molecular Cell
|June 11, 2013
PubMed
Summary

The RGG/RG motif, found in over 1,000 human proteins, plays crucial roles in gene regulation and cellular processes. Its involvement in disease highlights the importance of understanding these glycine-arginine-rich domains.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Glycine-arginine-rich (GAR) domains and RGG boxes are known functional motifs.
  • The RGG/RG motif is present in over 1,000 human proteins.
  • These motifs are implicated in various physiological processes.

Purpose of the Study:

  • To review the evolving functions of the RGG box and its variations, collectively termed the RGG/RG motif.
  • To discuss the role of the RGG/RG motif in mediating molecular interactions.
  • To highlight the motif's relevance in human diseases.

Main Methods:

  • Literature review of studies on RGG/RG motifs.
  • Analysis of the motif's involvement in physiological processes like transcription, splicing, DNA damage signaling, translation, and apoptosis.
  • Examination of RGG/RG motif's role in nucleic acid and protein interactions, including regulation by arginine methylation and partner-binding proteins.

Main Results:

  • The RGG/RG motif influences numerous cellular functions, including transcription, pre-mRNA splicing, DNA damage signaling, mRNA translation, and apoptosis regulation.
  • This motif mediates critical nucleic acid and protein interactions.
  • Arginine methylation and partner-binding proteins modulate RGG/RG motif functions.

Conclusions:

  • The RGG/RG motif is a functionally diverse and significant element in human proteins.
  • Its association with diseases such as neurological disorders, neuromuscular diseases, and cancer underscores its physiological importance.
  • Further research into the RGG/RG motif's emerging functionalities is warranted.