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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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...

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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

Structural aspects of Rab6-effector complexes.

Humberto Fernandes1, Edward Franklin, Rosario Recacha

  • 1School of Biochemistry and Immunology, Trinity College, Dublin 2, Ireland.

Biochemical Society Transactions
|September 17, 2009
PubMed
Summary
This summary is machine-generated.

The small GTPase Rab6, crucial for vesicle transport, binds distinct effectors like Rab6IP1 and GCC185. Structural analysis reveals how Rab6

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Identification of Post-translational Modifications of Plant Protein Complexes

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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

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Biology

Background:

  • The small GTPase Rab6 plays a critical role in regulating intracellular vesicle trafficking, particularly at the Golgi apparatus.
  • Understanding Rab6's interactions with its effectors is key to elucidating the molecular mechanisms of Golgi-mediated transport.

Purpose of the Study:

  • To determine the structural basis for Rab6's interaction with distinct effectors.
  • To elucidate the molecular mechanisms underlying Rab6's promiscuity in effector recruitment.

Main Methods:

  • X-ray crystallography was employed to solve the structures of Rab6 in complex with two different effectors: Rab6IP1 and GCC185.
  • Comparative structural analysis was performed on the determined complexes.

Main Results:

  • The crystal structures of Rab6a-GTP with Rab6-interacting protein 1 (Rab6IP1) and with the golgin GCC185 were determined.
  • In both complexes, effector binding involves two alpha-helices interacting with Rab6's switch I, switch II, and interswitch regions.
  • Conformational changes in Rab6's conserved hydrophobic triad were observed upon effector binding.

Conclusions:

  • The conformational flexibility of Rab6's hydrophobic triad allows it to recognize diverse alpha-helical coiled-coil effectors.
  • This flexibility provides a molecular explanation for Rab6's promiscuous nature in recruiting different effector proteins.