Molecular Characterization of Rab11 Interactions with Members of the Family of Rab11-interacting Proteins

Junutula, Jagath R.; Schonteich, Eric; Wilson, Gayle M.; Peden, Andrew A.; Scheller, Richard H.; Prekeris, Rytis

doi:10.1074/jbc.m404633200

Cited by 90 publications

(143 citation statements)

References 35 publications

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“…This is consistent with the studies by the Prekeris group (17). RH50 binding to Rab11 released more heat (ΔH=-39.5 kcal/mol) than RHNQ binding to Rab11 (ΔH=-25.8 kcal/mol), suggesting more polar interactions such as formation of hydrogen bonds or salt bridges.…”

Section: Discussionsupporting

confidence: 91%

“…The data presented in this paper provide significant insight into the interaction between Rab11 and the FIP2 family of interacting proteins complementing the work of others (17). While they provide much information on the molecular details of the interaction, the details remain to be answered at an atomic level.…”

Section: Discussionmentioning

confidence: 60%

“…Although appearing as a dimer in complex with FIP2, the oligomeric state of Rab11 alone is less well defined. While it was monomeric in solution by gel filtration experiments (17), it has been observed to be dimeric crystallographically (34) and diffusion measurements on Rab11 at 13 mg/ml using NMR spectroscopy show that it is a dimer (G.D. Henry & J.D. Baleja, unpublished results).…”

Section: Isothermal Titration Calorimetry Studiesmentioning

confidence: 97%

“…While a gel filtration experiment on RCP indicates a dimer (17), no one has determined the oligomerization state of FIP2. A cross-linking experiment was performed using the reagent BS 3 [Bis(sulfosuccinimidyl)suberate] (Figure 3).…”

Section: Oligomerization State Of the Fip2 Coiled-coil Domain By Crosmentioning

confidence: 99%

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Molecular Dissection of Rab11 Binding from Coiled-Coil Formation in the Rab11-FIP2 C-Terminal Domain

et al. 2006

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The Rab11-Family Interacting Protein (Rab11-FIP) group of effector proteins contain a highly conserved region in their C-termini that bind the GTPase, Rab11. Rab11 belongs to the largest family of small GTPases and is believed to regulate vesicle docking with target membranes and vesicle fusion. The amino acid sequence of the Rab11-FIP proteins predicts coiled-coil formation in the conserved C-terminal domain. In this study on Rab11-FIP2, we found experimental evidence for the coiled-coil and then defined the minimal structured core using limited proteolysis. We also showed that the Rab11-FIP2 coiled-coil domain forms a parallel homodimer in solution using cross-linking and mutagenesis and sedimentation equilibrium experiments. Various constructs representing the Cterminal domain of Rab11-FIP2 were characterized by circular dichroism and their affinity with Rab11 measured using isothermal titration calorimetry. The longest construct was both wellstructured and bound Rab11. A construct truncated at the N-terminus was poorly structured, but retained the same affinity for binding to Rab11. Conformational changes were also demonstrated upon complex formation between Rab11 and Rab11-FIP2. A construct truncated at the C-terminus, which was the minimal coiled-coil domain defined by limited proteolysis, did not retain the ability to interact with Rab11 although it was as well-structured as the longer peptide. These data show that coiled-coil formation and Rab11 binding are separable functions of the C-terminal domain of Rab11-FIP2. The dissection of Rab11 binding from the formation of defined structure in a coiled-coil provides a potential mechanism for regulating Rab11-dependent endosomal trafficking.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 60%

Section: Isothermal Titration Calorimetry Studiesmentioning

confidence: 97%

Section: Oligomerization State Of the Fip2 Coiled-coil Domain By Crosmentioning

confidence: 99%

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Molecular Dissection of Rab11 Binding from Coiled-Coil Formation in the Rab11-FIP2 C-Terminal Domain

et al. 2006

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“…Whether the SKIP PH domain:Rab9 interaction occurs in conjunction with phosphoinositides is not known, and the SKIP PH domain is the first shown to be bound to a RabGTPase. Measured affinities for Rab GTPases and their effectors range from nM to low M K d (21,(26)(27)(28). Further a K d of approximately 10 M has been reported for an analogous interaction between Rac GTPases 1, 2, and 3, and the PH domain of phospholipase C ␤2 protein (PLC-␤2) (29) and more recently a crystal structure of the PLC-␤2 PH:Rac 1 complex has been determined (30).…”

Section: Discussionmentioning

confidence: 99%

The Salmonella virulence protein SifA is a G protein antagonist

Jackson

Nawabi

Hentea

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Salmonella's success at proliferating intracellularly and causing disease depends on the translocation of a major virulence protein, SifA, into the host cell. SifA recruits membranes enriched in lysosome associated membrane protein 1 (LAMP1) and is needed for growth of Salmonella induced filaments (Sifs) and the Salmonella containing vacuole (SCV). It directly binds a host protein called SKIP (SifA and kinesin interacting protein) which is critical for membrane stability and motor dynamics at the SCV. SifA also contains a WxxxE motif, predictive of G protein mimicry in bacterial effectors, but whether and how it mimics the action of a host G protein is not known. We show that SKIP's pleckstrin homology domain, which directly binds SifA, also binds to the late endosomal GTPase Rab9. Knockdown studies suggest that both SKIP and Rab9 function to maintain peripheral LAMP1 distribution in cells. The Rab9:SKIP interaction is GTP-dependent and is inhibited by SifA binding to the SKIP pleckstrin homology domain, suggesting that SifA may be a Rab9 antagonist. SifA:SKIP binding is significantly tighter than Rab9:SKIP binding and may thus allow SifA to bring SKIP to the SCV via SKIP's Rab9-binding site. Rab9 can measurably reverse SifA-dependent LAMP1 recruitment and the perinuclear location of the SCV in cells. Importantly, binding to SKIP requires SifA residues W197 and E201 of the conserved WxxxE signature sequence, leading to the speculation that bacterial G protein mimicry may result in G protein antagonism.GTPase ͉ LAMP1 ͉ Rab9 ͉ SKIP ͉ lysosome

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FIP 5 phosphorylation during mitosis regulates apical trafficking and lumenogenesis

et al. 2014

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Apical lumen formation is a key step during epithelial morphogenesis. The establishment of the apical lumen is a complex process that involves coordinated changes in plasma membrane composition, endocytic transport, and cytoskeleton organization. These changes are accomplished, at least in part, by the targeting and fusion of Rab11/FIP5-containing apical endosomes with the apical membrane initiation site (AMIS). Although AMIS formation and polarized transport of Rab11/FIP5-containing endosomes are crucial for the formation of a single apical lumen, the spatiotemporal regulation of this process remains poorly understood. Here, we demonstrate that the formation of the midbody during cytokinesis is a symmetry-breaking event that establishes the location of the AMIS. The interaction of FIP5 with SNX18, which is required for the formation of apical endocytic carriers, is inhibited by GSK-3 phosphorylation at FIP5-T276. Importantly, we show that FIP5-T276 phosphorylation occurs specifically during metaphase and anaphase, to ensure the fidelity and timing of FIP5-endosome targeting to the AMIS during apical lumen formation.

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Molecular Characterization of Rab11 Interactions with Members of the Family of Rab11-interacting Proteins

Cited by 90 publications

References 35 publications

Molecular Dissection of Rab11 Binding from Coiled-Coil Formation in the Rab11-FIP2 C-Terminal Domain

Molecular Dissection of Rab11 Binding from Coiled-Coil Formation in the Rab11-FIP2 C-Terminal Domain

The Salmonella virulence protein SifA is a G protein antagonist

FIP 5 phosphorylation during mitosis regulates apical trafficking and lumenogenesis

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