Disease relevance of RAB11FIP3

• Furthermore, in rat dorsal root ganglion cells, the rat eferin homologue also colocalizes with rVR1 [1].

High impact information on RAB11FIP3

• Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis [2].
• Third, we show that the Rab11-FIP3 complex is required for a late stage of cytokinesis, possibly abscission [3].
• Second, we demonstrate that the Rab11-FIP3 protein complex is intimately involved in the delivery of endosomes to the cleavage furrow [3].
• The binding of Rab11-FIP1, Rab11-FIP2, and Rab11-FIP3 to Rab11a was dependent upon a conserved carboxyl-terminal amphipathic alpha-helix [4].
• GFP-Rab11-FIP3 also colocalized with Rab11a in HeLa cells [4].

Biological context of RAB11FIP3

• It is likely that Rab11-FIP3 is involved in trafficking events other than Tfn trafficking; these may include the transport of endosomally derived membrane to the cleavage furrow during cytokinesis [5].
• Rab11-FIP3 and Rab11-FIP4 possess an ezrin-radixin-moesin (ERM) domain in their C-terminal half and EF hands in their N-terminal region [6].

Anatomical context of RAB11FIP3

• We have demonstrated that both Rab11 and Rab11-FIP3 localise to the cleavage furrow during cytokinesis, and that Rab11-FIP3 localisation is dependent on both microtubule and actin filament integrity [5].
• Here we describe the purification of Rab11-FIP3 and report its biological properties in eukaryotic cells as visualized by immunofluorescence microscopy [7].
• This was determined by two-electrode recording of oocytes and whole cell recording of HEK cells that were cotransfected with VR1 and human eferin [1].

Associations of RAB11FIP3 with chemical compounds

• We show that Rab11-FIP3 does not enter brefeldin A (BFA) induced membrane tubules that are positive for the transferrin receptor (TfnR) [5].

Physical interactions of RAB11FIP3

• Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins [8].

Other interactions of RAB11FIP3

• Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis [5].
• Furthermore, we show that expression of an amino-terminally truncated mutant of Rab11-FIP3 (Rab11-FIP3((244-756))) does not inhibit transferrin (Tfn) recycling in HeLa cells [5].
• We now demonstrate that two of the family members-pp75/Rip11 and Rab11-FIP3 do not bind Rab4 and show that several members of the family can self-interact and interact with each other [9].

Analytical, diagnostic and therapeutic context of RAB11FIP3

• Utilising a polyclonal antibody specific for Rab11-FIP3, we have demonstrated by immunofluorescence microscopy that Rab11-FIP3 colocalises with Rab11 in a distinctive pericentrosomal location in A431 cells [5].

References