Involvement of a Rab8-like protein of Dictyostelium discoideum, Sas1, in the formation of membrane extensions, secretion and adhesion during development

Powell, Rhonda R.; Temesvari, Lesly A.

doi:10.1099/mic.0.27073-0

Cited by 21 publications

(25 citation statements)

References 48 publications

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“…A cessation of this membrane-recycling pathway would promote plasma membrane stabilization and cell-cell adhesion. This process is likely to be evolutionary well preserved because a dominant-negative mutant of the Rab8-like protein of Dictyostelium discoideum, Sas1, also promotes cell-cell adhesion (Powell and Temesvari, 2004). Our hypothesis is in accordance with the role of Rab8 in neurite outgrowth and development of photoreceptors (Huber et al, 1995;Kametani et al, 2003;Moritz et al, 2001;Deretic et al, 2004).…”

Section: Discussionsupporting

confidence: 78%

Characterization of the Rab8-specific membrane traffic route linked to protrusion formation

Hattula

Furuhjelm

Tikkanen

et al. 2006

Journal of Cell Science

209

294

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Rab8 has a drastic effect on cell shape, but the membrane trafficking route it regulates is poorly defined. Here, we show that endogenous and ectopically expressed Rab8 is associated with macropinosomes generated at ruffling membrane domains. These macropinosomes fuse or transform into tubules that move toward the cell center, from where they are recycled back to the leading edge. The biogenesis of these tubules is dependent on actin and microtubular dynamics. Expression of dominant-negative Rab8 mutants or depletion of Rab8 by RNA interference inhibit protrusion formation, but promote cell-cell adhesion and actin stress fiber formation, whereas expression of the constitutively active Rab8-Q67L has the opposite effect. Rab8 localization overlaps with both Rab11 and Arf6, and is functionally linked to Arf6. We also demonstrate that Rab8 activity is needed for the transport of transferrin and the transferrin receptor to the pericentriolar region and to cell protrusions, and that Rab8 controls the traffic of cholera toxin B to the Golgi compartment. Finally, Rab8 colocalizes and binds specifically to a synaptotagmin-like protein (Slp1/JFC1), which is involved in controlling Rab8 membrane dynamics. We propose that Rab8 regulates a membrane-recycling pathway that mediates protrusion formation.

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Section: Discussionsupporting

confidence: 78%

Characterization of the Rab8-specific membrane traffic route linked to protrusion formation

Hattula

Furuhjelm

Tikkanen

et al. 2006

Journal of Cell Science

209

294

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“…While Rab8 localizes to the trans-Golgi network, recycling endosomes, vesicular and tubular structures in the cytosol, membrane protrusions, and plasma membrane (PM) in addition to AJs (Huber et al, 1993b;Lau and Mruk, 2003;Ang et al, 2004), Rab13 resides at perinuclear membrane structures, vesicular structures in the cytosol, and PM in addition to TJs (Zahraoui et al, 1994;Marzesco et al, 2002;Terai et al, 2006). Rab8 interacts with Rab8ip/germinal center kinase (GCK), JFC1/Slp1, and Optineurin in a GTP-dependent manner (Ren et al, 1996;Hattula and Peränen, 2000;Hattula et al, 2006), and it is implicated in multiple transport pathways, including the epithelial-specific adaptor protein complex AP-1B-dependent basolateral transport, the polarized membrane traffic to the dendritic membrane, the actin-dependent movement of melanosomes, the formation and destruction of membrane protrusions, and the cell-cell adhesion (Huber et al, 1993a;Ang et al, 2003;Powell and Temesvari, 2004;Chabrillat et al, 2005;Hattula et al, 2006). Rab13 also binds to protein kinase A (PKA), and it regulates the assembly of functional TJs, neurite outgrowth, and neuronal regeneration (Marzesco et al, 2002;Kö hler et al, 2004;Di Giovanni et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

The Interaction of JRAB/MICAL-L2 with Rab8 and Rab13 Coordinates the Assembly of Tight Junctions and Adherens Junctions

Yamamura

Nishimura²,

Nakatsuji³

et al. 2008

MBoC

102

120

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The assembly of tight junctions (TJs) and adherens junctions (AJs) is regulated by the transport of integral TJ and AJ proteins to and/or from the plasma membrane (PM) and it is tightly coordinated in epithelial cells. We previously reported that Rab13 and a junctional Rab13-binding protein (JRAB)/molecule interacting with CasL-like 2 (MICAL-L2) mediated the endocytic recycling of an integral TJ protein occludin and the formation of functional TJs. Here, we investigated the role of Rab13 and JRAB/MICAL-L2 in the transport of other integral TJ and AJ proteins claudin-1 and E-cadherin to the PM by using a Ca2+-switch model. Although knockdown of Rab13 specifically suppressed claudin-1 and occludin but not E-cadherin transport, knockdown of JRAB/MICAL-L2 and expression of its Rab13-binding domain (JRAB/MICAL-L2-C) inhibited claudin-1, occludin, and E-cadherin transport. We then identified Rab8 as another JRAB/MICAL-L2-C-binding protein. Knockdown of Rab8 inhibited the Rab13-independent transport of E-cadherin to the PM. Rab8 and Rab13 competed with each other for the binding to JRAB/MICAL-L2 and functionally associated with JRAB/MICAL-L2 at the perinuclear recycling/storage compartments and PM, respectively. These results suggest that the interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of AJs and TJs.

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“…The purity of GST and GST fusion proteins was assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and silver staining as described previously (29). Western blot analysis was performed as described previously (44) to verify the authenticity of GST-tagged proteins using a 1:10,000 dilution of anti-GST antibodies (Chemicon, Temecula, CA).…”

Section: Btkmentioning

confidence: 99%

Localization of Phosphatidylinositol (3,4,5)-Trisphosphate to Phagosomes in Entamoeba histolytica Achieved Using Glutathione S -Transferase- and Green Fluorescent Protein-Tagged Lipid Biosensors

et al. 2010

Self Cite

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Entamoeba histolytica is an intestinal protozoan parasite that causes amoebic dysentery and liver abscess. Phagocytosis by the parasite is a critical virulence process, since it is a prerequisite for tissue invasion and establishment of chronic infection. While the roles of many of the proteins that regulate phagocytosis-related signaling events in E. histolytica have been characterized, the functions of lipids in this cellular process remain largely unknown in this parasite. In other systems, phosphatidylinositol (3,4,5)-trisphosphate (PIP 3 ), a major product of phosphoinositide 3 kinase (PI3-kinase) activity, is essential for phagocytosis. Pleckstrin homology (PH) domains are protein domains that specifically bind to PIP 3 . In this study, we utilized glutathione S-transferase (GST)-and green fluorescent protein (GFP)-labeled PH domains as lipid biosensors to characterize the spatiotemporal aspects of PIP 3 distribution during various endocytic processes in E. histolytica. PIP 3 -specific biosensors accumulated at extending pseudopodia and in phagosomal cups in trophozoites exposed to erythrocytes but did not localize to pinocytic compartments during the uptake of a fluid-phase marker, dextran. Our results suggest that PIP 3 is involved in the early stages of phagosome formation in E. histolytica. In addition, we demonstrated that PIP 3 exists at high steady-state levels in the plasma membrane of E. histolytica and that these levels, unlike those in mammalian cells, are not abolished by serum withdrawal. Finally, expression of a PH domain in trophozoites inhibited erythrophagocytosis and enhanced motility, providing genetic evidence supporting the role of PI3-kinase signaling in these processes in E. histolytica.Entamoeba histolytica is an intestinal protozoan parasite that causes amoebic dysentery and liver abscess. A high incidence of E. histolytica infection is found in developing countries and is associated with low basic hygiene standards and a lack of water sanitation (reviewed in reference 20). Since E. histolytica is mainly a human parasite (40), improvements in sanitation may help prevent the fecal-oral spread of this pathogen; however, overpopulation, scarcity of clean water, and socioeconomic shortcomings impede the progress of such improvements in developing countries (36). This lack of progress supports an elevated need for the development of improved prevention, diagnosis, and treatment for dysentery caused by E. histolytica. This requires a better understanding of the basic biology of this parasite.

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Involvement of a Rab8-like protein of Dictyostelium discoideum, Sas1, in the formation of membrane extensions, secretion and adhesion during development

Cited by 21 publications

References 48 publications

Characterization of the Rab8-specific membrane traffic route linked to protrusion formation

Characterization of the Rab8-specific membrane traffic route linked to protrusion formation

The Interaction of JRAB/MICAL-L2 with Rab8 and Rab13 Coordinates the Assembly of Tight Junctions and Adherens Junctions

Localization of Phosphatidylinositol (3,4,5)-Trisphosphate to Phagosomes in Entamoeba histolytica Achieved Using Glutathione S -Transferase- and Green Fluorescent Protein-Tagged Lipid Biosensors

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