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Related Concept Videos

Rab Proteins01:14

Rab Proteins

5.3K
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...
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Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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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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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Rab Cascades01:25

Rab Cascades

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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.
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Updated: Mar 6, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

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Grb7 protein RA domain oligomerization.

Malika P Godamudunage1,2, Albert Foster3, Darius Warren4

  • 1Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI, USA.

Journal of Molecular Recognition : JMR
|March 16, 2017
PubMed
Summary
This summary is machine-generated.

The ras associating and pleckstrin homology (RA) domain of growth factor receptor bound protein 7 (Grb7) can form transient multimeric structures. This oligomerization may play a key role in Grb7

Keywords:
Grb7RAPH domainscancercell migrationoligomerization

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Last Updated: Mar 6, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

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A High-content Imaging Workflow to Study Grb2 Signaling Complexes by Expression Cloning
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A High-content Imaging Workflow to Study Grb2 Signaling Complexes by Expression Cloning

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Growth factor receptor bound protein 7 (Grb7) is an adaptor protein frequently coamplified in breast cancer.
  • Grb7 overexpression correlates with increased cell migration and metastasis.
  • The ras associating and pleckstrin homology (RA) domain of Grb7 interacts with downstream signaling proteins, influencing cell migration.

Purpose of the Study:

  • To investigate the oligomeric state of the Grb7 RA domain.
  • To determine the functional significance of Grb7 RA domain oligomerization in Grb7-mediated cell migration.

Main Methods:

  • Size exclusion chromatography
  • Nuclear magnetic resonance (NMR) and nuclear relaxation studies
  • Glutaraldehyde cross-linking and dynamic light scattering (DLS)

Main Results:

  • The Grb7 RA domain exists in transient multimeric forms.
  • Oligomerization of the Grb7 RA domain is potentially linked to Grb7's role in cell migration.

Conclusions:

  • The Grb7 RA domain exhibits oligomerization.
  • This oligomerization may be a critical factor in Grb7's function in cell migration and cancer progression.