The interaction sites of Rab proteins are located at different positions in the coiled-coil region and do not appear to be essential for the recruitment of GRIP proteins to the Golgi membranes.
ARFRP1 is required for the recruitment of ARL1 and its effector, the GRIP domain protein Golgin-245, to trans-Golgi membranes (7, 9, 10).
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GRIP domain proteins and ARL-1 under both GDP and GTP forms are localised to the TGN.
In the current model (described in yeast but applicable to mammals), the GDP-bound form of Scarl-1p (HsARL-1) is cytoplasmic; when GDP is exchanged with GTP under the action of the nucleotide exchange factor, Scarl-1p (HsARL-1) moves to the Golgi membranes and recruits GRIP domain proteins [30] [62], [62].
Since the «empty form» and GRIP domain proteins probably do not interact physically, these cytoplasmic localisations probably represent a common consequence of the TGN destabilisation, whixh may not be complete since ARF-1-mRed localisation did not change (within the limits of the fluorescence micoscopy resolution).
Interestingly, the subcellular distribution of the GRIP-containing protein Cbs in developing Drosophila varies during the cell division cycle from GA to chromosomes and centrosomes in the mitotic spindle [ 35].
The proteoglycan present on the NG2 cell membrane, together with the glutamate receptor interacting protein (GRIP), forms the NG2-GRIP-AMPA receptor complexes, which are involved in the alignment and formation of the neuron-NG2 cell synapse [ 30].
The GTP form may recruit GRIP-domain proteins from the Golgi soluble compartment to Golgi membranes and the GDP form releases them.
For example, the first and second PDZ domains (PDZ12) of GRIP-1 proteins are connected in this way.
NMDA receptors have been found to bind to the PSD-95 family of proteins, whereas AMPA receptors interact with the PDZ-domain-containing protein GRIP (glutamate receptor interacting protein).
