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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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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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Activation and Inactivation of G Proteins01:22

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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...
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Small GTPases - Ras and Rho01:24

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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.
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Rab Cascades01:25

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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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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
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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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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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The TRAPP complexes: discriminating GTPases in context.

Saket R Bagde1, J Christopher Fromme1

  • 1Department of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY, USA.

FEBS Letters
|December 9, 2022
PubMed
Summary
This summary is machine-generated.

Guanine-nucleotide exchange factors (GEFs) like TRAPP complexes ensure Rab GTPases reach their correct cellular locations. Membrane surfaces critically influence these GEF-GTPase interactions, guiding proper cell function.

Keywords:
GTPaseRabTRAPPguanine-nucleotide exchange factormembrane trafficking

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Rab GTPases are essential for membrane trafficking, and their correct localization is crucial for cellular function.
  • Guanine-nucleotide exchange factors (GEFs) dictate Rab localization by activating them on specific membranes.
  • TRAPP complexes (TRAPPII and TRAPPIII) are GEFs that activate distinct Rabs (Rab11 and Rab1) using the same catalytic site.

Purpose of the Study:

  • To review recent findings on Rab substrate selection mechanisms by TRAPP complexes.
  • To highlight the role of the Rab C-terminal hypervariable domain (HVD) in specificity.
  • To emphasize the importance of the membrane surface in GEF-GTPase interactions.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) studies of yeast and metazoan TRAPP complexes.
  • Analysis of Rab C-terminal hypervariable domain (HVD) length as a specificity determinant.
  • Biochemical and structural analyses of GEF-GTPase interactions.

Main Results:

  • TRAPP complexes utilize specific mechanisms to select and activate Rab substrates.
  • The HVD of Rabs, particularly its length, is a key factor in TRAPP complex specificity.
  • Membrane surfaces provide essential contextual information for GEF-GTPase binding and activation.

Conclusions:

  • Understanding Rab-GEF interactions is key to deciphering membrane trafficking pathways.
  • TRAPP complexes exhibit sophisticated substrate recognition, influenced by Rab HVD and membrane context.
  • Recent structural insights from cryo-EM have advanced our knowledge of these critical cellular processes.