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Rab-Guanosine biphosphate Dissociation Inhibitor (or Rab-GDI) is an inhibitory protein which facilitated extraction of prenylated GDP-bounds inactive conformation of Rab small GTPase from membranes. This molecule has an important role in vesicular membrane trafficking. It delivers Rab to new formes vesicles (for exocytic and endocytic pathways), where it becomes activated to the GTP-bound form to promote the recuitment of effectors that facilitate vesicle transport through the cytoplasm by the cytoskeleton. This inhibition can be removed by the action of a GEF.
Rab-Guanosine biphosphate Dissociation Inhibitor (or Rab-GDI) is an inhibitory protein which facilitated extraction of prenylated GDP-bounds inactive conformation of Rab small GTPase from membranes. This molecule has an important role in vesicular membrane trafficking. It delivers Rab to new formes vesicles (for exocytic and endocytic pathways), where it becomes activated to the GTP-bound form to promote the recuitment of effectors that facilitate vesicle transport through the cytoplasm by the cytoskeleton. This inhibition can be removed by the action of a GEF.




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Rab-GDI does not facilitate Rab prenylation, but serves as a generic regulator for recycling of rab-GTPases for use in multiple rounds of membrane transport. It retrieves Rabs  from the membrane and delivers it to the cytosol, controlling the distribution of Rabs between membranes and cytosol. GDI is believed to be stably associated only with GDP-loaded and prenylated Rabs proteins, ensuring retrieval of inactivated Rab GTPases from the membrane at the end of their functionnal cycle. Rab-GDI is critically important for the proper functionning of the vesicular transport machinery, and its deletion can be lethal.
Rab-GDI does not facilitate Rab prenylation, but serves as a generic regulator for recycling of rab-GTPases for use in multiple rounds of membrane transport. It retrieves Rabs  from the membrane and delivers it to the cytosol, controlling the distribution of Rabs between membranes and cytosol. GDI is believed to be stably associated only with GDP-loaded and prenylated Rabs proteins, ensuring retrieval of inactivated Rab GTPases from the membrane at the end of their functionnal cycle. Rab-GDI is critically important for the proper functionning of the vesicular transport machinery, and its deletion can be lethal.


= Structure =
= Structure =

Revision as of 17:06, 1 December 2011

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Rab-Guanosine biphosphate Dissociation Inhibitor (or Rab-GDI) is an inhibitory protein which facilitated extraction of prenylated GDP-bounds inactive conformation of Rab small GTPase from membranes. This molecule has an important role in vesicular membrane trafficking. It delivers Rab to new formes vesicles (for exocytic and endocytic pathways), where it becomes activated to the GTP-bound form to promote the recuitment of effectors that facilitate vesicle transport through the cytoplasm by the cytoskeleton. This inhibition can be removed by the action of a GEF.


Biological roleBiological role

Rab-GDI does not facilitate Rab prenylation, but serves as a generic regulator for recycling of rab-GTPases for use in multiple rounds of membrane transport. It retrieves Rabs from the membrane and delivers it to the cytosol, controlling the distribution of Rabs between membranes and cytosol. GDI is believed to be stably associated only with GDP-loaded and prenylated Rabs proteins, ensuring retrieval of inactivated Rab GTPases from the membrane at the end of their functionnal cycle. Rab-GDI is critically important for the proper functionning of the vesicular transport machinery, and its deletion can be lethal.

StructureStructure

General structureGeneral structure

Substrate binding and catalytic mechanismSubstrate binding and catalytic mechanism

Regulation ???Regulation ???

DiseasesDiseases

Additional 3D Structures of Rab GDP-Dissociation InhibitorAdditional 3D Structures of Rab GDP-Dissociation Inhibitor

Additional ressourcesAdditional ressources

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Charlotte Simonin, Lucie Maubert