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Related Concept Videos

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.
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...
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:
GTPases and their Regulation02:14

GTPases and their Regulation

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.
Large G-proteins, also known...
GTPases and their Regulation02:14

GTPases and their Regulation

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.
Large G-proteins, also known...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

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Related Experiment Video

Updated: May 21, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

A Ypt/Rab GTPase module makes a PAS.

Zhanna Lipatova1, Nava Segev

  • 1Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, IL, USA.

Autophagy
|June 7, 2012
PubMed
Summary
This summary is machine-generated.

Ypt/Rab GTPases coordinate cellular trafficking. Our study identifies Atg11 as a Ypt1 effector, revealing how Ypt1 GTPase regulates autophagy and ER-to-Golgi transport by interacting with the TRAPP complex at the phagophore assembly site.

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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Related Experiment Videos

Last Updated: May 21, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Ypt/Rab GTPases organize membrane micro-domains, crucial for eukaryotic membrane trafficking.
  • Autophagy, a membrane trafficking process, is increasingly linked to Ypt/Rab GTPase functions.
  • The precise mechanisms and coordination roles of Ypt/Rabs in autophagy remain unclear.

Purpose of the Study:

  • To elucidate the role and mechanism of Ypt/Rab GTPases in autophagy.
  • To investigate how Ypt/Rabs coordinate autophagy with other cellular trafficking pathways, such as ER-to-Golgi transport.
  • To identify downstream effectors of Ypt GTPases involved in autophagy.

Main Methods:

  • Investigated the interaction between Ypt1, TRAPP complex, and Atg11.
  • Utilized yeast models for studying selective autophagy and phagophore assembly site (PAS) formation.
  • Analyzed the functional requirement of the Ypt1 GTPase module in autophagy.

Main Results:

  • Identified Atg11, a phagophore assembly site (PAS) component, as a downstream effector of yeast Ypt1.
  • Demonstrated that the Ypt1 activator (TRAPP complex), Ypt1, and Atg11 interact on the PAS.
  • Showed that this GTPase module is essential for PAS formation during selective autophagy.

Conclusions:

  • Ypt/Rab GTPases coordinate the secretory and autophagic pathways.
  • This coordination is achieved by recruiting specific effectors for each pathway.
  • Atg11 acts as a key effector for Ypt1 in regulating autophagy.