Rab GTPases as coordinators of vesicle traffic

  title={Rab GTPases as coordinators of vesicle traffic},
  author={Harald A Stenmark},
  journal={Nature Reviews Molecular Cell Biology},
  • H. Stenmark
  • Published 1 August 2009
  • Biology
  • Nature Reviews Molecular Cell Biology
Membrane trafficking between organelles by vesiculotubular carriers is fundamental to the existence of eukaryotic cells. Central in ensuring that cargoes are delivered to their correct destinations are the Rab GTPases, a large family of small GTPases that control membrane identity and vesicle budding, uncoating, motility and fusion through the recruitment of effector proteins, such as sorting adaptors, tethering factors, kinases, phosphatases and motors. Crosstalk between multiple Rab GTPases… 

Rab regulation by GEFs and GAPs during membrane traffic.

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The regulation of Rab GTPases by proteins that control their membrane association and activation state is highlighted and an overview of the cellular processes that are regulated by Rab G TPases and their effectors, including protein sorting, vesicle motility and vesicles tethering is provided.

Rab proteins and the compartmentalization of the endosomal system.

The roles of Rab GTPases in compartmentalization of the endocytic pathway into early, recycling, late, and lysosomal routes, coordination of individual transport steps, and integration of GTPase and signaling cascades are discussed.

Rab GTPases: Central Coordinators of Membrane Trafficking in Cancer

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Rabs and EHDs: alternate modes for traffic control.

By comparing and contrasting key aspects in their modes of function, this work shall promote a better understanding of how Rab proteins and EHDs regulate endocytic trafficking.

Rab GTPase regulation of membrane identity.

  • S. Pfeffer
  • Biology
    Current opinion in cell biology
  • 2013

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A review provides a summary of various post translational modifications (PTMs) and their significance to regulate localization and function of different Rabs.

Rab11 in Disease Progression

An overview over Rab11 subfamily is described with a brief structural aspect and its roles in implicating different disease progression.

Rab GTPases and Their Interacting Proteins in Health and Disease

The discovery, evolution and characterization of the Rab GTPase family are discussed, including their basic functional roles, their important structural features and the regulatory proteins which mediate Rab function.



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TIP47 bound directly to the Rab9 guanosine triphosphatase (GTPase) in its active, GTP-bound conformation, and Rab9 increased the affinity of TIP47 for its cargo.

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Cellular organelles in the exocytic and endocytic pathways have a distinctive spatial distribution and communicate through an elaborate system of vesiculo-tubular transport. Rab proteins and their

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The reconstitution of the selec-tive targeting of prenylated Rab9 protein onto late endosome mem-branes is described and it is shown that this process is accompanied by endosomes-triggered nucleotide exchange.

Interaction of a Golgi-associated kinesin-like protein with Rab6.

A molecular motor is a potential effector of a Rab protein, and coordinated action between members of these two families of proteins could control membrane dynamics and directional vesicular traffic.

Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion.

It is proposed that Rab1-regulated assembly of functional effector-SNARE complexes defines a conserved molecular mechanism to coordinate recognition between subcellular compartments.

Ubiquitin binding and conjugation regulate the recruitment of Rabex‐5 to early endosomes

It is demonstrated that Ub binding is essential for the recruitment of Rabex‐5 from the cytosol to endosomes, independently of its GEF activity and of Rab5.

Structural basis of family-wide Rab GTPase recognition by rabenosyn-5

The results demonstrate that even the structurally similar effector domains in rabenosyn-5 can achieve highly selective recognition of distinct subsets of Rab GTPases exclusively through interactions with the switch and interswitch regions.

Rab5 regulates motility of early endosomes on microtubules

A new role for Rab5 is revealed in the regulation of endosome interactions with the microtubule network using Rab5 fused to green fluorescent protein and it is shown that Rab5-positive endosomes move on microtubules in vivo.

Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes

This work reports the reconstitution of the early endosomal canine Rab5 GTPase, its key regulators and effectors together with SNAREs into proteoliposomes using a set of 17 recombinant human proteins.

Rab GTPases and Myosin Motors in Organelle Motility

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