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Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization and maturation of recycling endosomes.

Authors: Hoogenraad, Casper C  Popa, Ioana  Futai, Kensuke  Martinez-Sanchez, Emma  Wulf, Phebe S  van Vlijmen, Thijs  Dortland, Bjorn R  Oorschot, Viola  Govers, Roland  Monti, Maria  Heck, Albert J R  Sheng, Morgan  Klumperman, Judith  Rehmann, Holger  Jaarsma, Dick  Kapitein, Lukas C  van der Sluijs, Peter 
Citation: Hoogenraad CC, etal., PLoS Biol. 2010 Jan 19;8(1):e1000283. doi: 10.1371/journal.pbio.1000283.
Pubmed: (View Article at PubMed) PMID:20098723
DOI: Full-text: DOI:10.1371/journal.pbio.1000283

The endosomal pathway in neuronal dendrites is essential for membrane receptor trafficking and proper synaptic function and plasticity. However, the molecular mechanisms that organize specific endocytic trafficking routes are poorly understood. Here, we identify GRIP-associated protein-1 (GRASP-1) as a neuron-specific effector of Rab4 and key component of the molecular machinery that coordinates recycling endosome maturation in dendrites. We show that GRASP-1 is necessary for AMPA receptor recycling, maintenance of spine morphology, and synaptic plasticity. At the molecular level, GRASP-1 segregates Rab4 from EEA1/Neep21/Rab5-positive early endosomal membranes and coordinates the coupling to Rab11-labelled recycling endosomes by interacting with the endosomal SNARE syntaxin 13. We propose that GRASP-1 connects early and late recycling endosomal compartments by forming a molecular bridge between Rab-specific membrane domains and the endosomal SNARE machinery. The data uncover a new mechanism to achieve specificity and directionality in neuronal membrane receptor trafficking.

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CRRD Object Information
CRRD ID: 12050105
Created: 2017-01-21
Species: All species
Last Modified: 2017-01-21
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.