Notch receptors are clustered and trans-endocytosed by Delta ligand cells. Confocal micrograph of a Delta expressing cell (left) interacting with a Notch expressing cell (right). Following interaction with Delta (blue), cell surface Notch (yellow) is clustered at cell-cell interfaces. Notch extracellular domain is detected within Delta cells (green) indicative of trans-endocytosis. Endocytosis of ligand while bound to Notch may produce a force sufficient to pull Notch apart and activate signaling.
 
 
 
 
 
 

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Volume 8 issue 4 April 2007
Rab11-FIP3 is critical for the structural integrity of the endosomal-recycling compartment
Conor P. Horgan, Arkadiusz Oleksy, Alexander V. Zhdanov, Patrick Y. Lall, Ian J. White, Amir R. Khan, Clare E. Futter, John G. McCaffrey and Mary W. McCaffrey

Figure 1: RME-1 colocalises with Rab11-FIP3 on the ERC. A431 cells were transfected with pEGFP-C1/Rab11-FIP3 WT. Eighteen hours post-transfection the cells were processed for immunofluorescence and immunostained with an antibody to RME-1. These data are typical of three separate experiments. Scale bar represents 10 µm.

Figure 1 (jpg)

Figure 2: Rab11-FIP3 I738E expression disrupts the pericentrosomal ERC. A431 cells were transfected with pEGFP-C1/Rab11-FIP3 I738E. Sixteen to eighteen hours post-transfection the cells were processed for immunofluorescence and immunostained with antibodies to RCP or Rab11-FIP4. These data are typical of four separate experiments. Scale bar represents 10 µm.

Figure 2 (jpg)

Figure 3: Rab11-FIP3 is predicted to form extensive α-helical coiled-coil structures. (A) Overlay of plots depicting the probability of forming α-helical coiled-coil structures in Rab11-FIP3 as determined using PairCoil algorithm (blue) and disorder probability using DISOPRED2 (red). Regions above the dashed line on the DISOPRED2 plot are considered disordered. (B) Overlay of plots depicting the probability that Rab11-FIP3 will form a dimeric (blue) or trimeric (green) coiled-coil structure as determined using the MultiCoil algorithm.

Figure 3 (jpg)

Figure 4: ClustalW alignment of the Rab11-FIPs. (A) ClustalW alignment of the class II Rab11-FIPs. Identities are in black and similarities are in grey. Amino acid residues 463-692 of Rab11-FIP3 are underlined in blue. The region of Rab11-FIP3 for which the crystal structure has been solved is underlined in red. (B) ClustalW alignment of the class I Rab11-FIPs with Rab11-FIP3. Identities are in black and similarities are in grey. Amino acid residues 463-692 of Rab11-FIP3 are underlined in blue.

Figure 4 (jpg)

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