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  • receptors
  • and Tall, Alan R., "Free cholesterol accumulation in macrophage membranes activates Toll-like receptors and p38 mitogen-activated protein kinase and induces cathepsin K" (2009). (umassmed.edu)
  • Sensory functions of primary cilia rely on ciliary-localized membrane proteins, but little is known about how these receptors are targeted to the cilium. (nih.gov)
  • 2001
  • 2001). CG31064, the Drosophila ortholog of these proteins, showed a strong and highly specific interaction with Rab4 under both lysis conditions (which we confirmed to be GTP-specific using a GFP-tagged CG31064), indicating that the Rab4-GTP was functional (Figures 4A and 4B). (nih.gov)
  • 2001). In addition, the putative catalytic residues (R559, Y592, and Q594) of TBC1D9B were exposed similarly to those of TBC1D4 and other TBC proteins such as Gyp1p (unpublished data). (nih.gov)
  • 2001), protein enrichment at specific sites on the plasma membrane relies on protein and lipid-mediated signaling networks and follows temporal and spatial hierarchies of molecular interactions. (nih.gov)
  • 2001). A vertex ring of proteins and lipids assembles on tethered vacuoles before catalyzing fusion (Wang et al. (nih.gov)
  • vesicle transport
  • Rab proteins are key mediators of vesicle transport and specificity, and via the presence of multiple paralogues, alterations in interaction specificity and modification of pathways, contribute greatly to the evolution of complexity of membrane transport. (nih.gov)
  • GTPase Ypt7p
  • Yeast vacuole fusion requires 4 SNAREs, the Rab GTPase Ypt7p, vacuolar lipids, the SNARE complex disassembly machinery Sec17p and Sec18p, and the heterohexameric HOPS complex. (dartmouth.edu)
  • vacuole fusion
  • Vacuole fusion occurs in stages: cis-SNARE complexes (bound to one. (dartmouth.edu)
  • Though we have only used a select few inhibitors and GFP-tagged a subset of the proteins that catalyze vacuole fusion (Wickner, 2002), their interplay has revealed the first outlines of a vertex ring assembly hierarchy. (nih.gov)
  • actin
  • These findings suggest that PI(3,5)P2 formation on endosomes may remove cortactin from endosome-associated branched actin.Conversely, inhibition of Arp2/3 complex activity greatly reduced cortactin localization to late endosomes.These data suggest a model in which PI(3,5)P2 binding removes cortactin from late endosomal branched actin networks and thereby promotes net actin turnover. (nih.gov)
  • Two candidates for mediating this actin-based process are the Arp2/3 complex and formin family proteins. (dartmouth.edu)
  • and (d) The t-SNAREs regulate the vertex enrichment of both G-actin and the Ypt7p effector complex for homotypic fusion and vacuole protein sorting (HOPS).In accord with this hierarchy concept, the HOPS complex, at the end of the vertex assembly hierarchy, is most enriched at those vertices with abundant Ypt7p, which is at the start of the hierarchy. (nih.gov)
  • and (d) The t-SNAREs regulate the vertex enrichment of both G-actin and the Ypt7p effector complex for homotypic fusion and vacuole protein sorting (HOPS). (nih.gov)
  • 2002). We have now identified a hierarchy in the spatial localization of these docking and fusion factors, revealing new features of the interactions between organelle-bound actin, Ypt/Rab GTPase, and SNAREs (Fig. 8). (nih.gov)
  • Superfamily
  • They are both classified in the SCOP hierarchy as FAD/NAD(P)-binding domain fold and superfamily, which suggests a common ancestry. (nih.gov)
  • cells
  • B) Anti-GFP immunoblot of affinity chromatography of lysates from S2 cells expressing GFP-CG31064 (FYVE domain form) or CG7371-GFP using GDP- and GTP-locked Rabs. (nih.gov)
  • The proteins are human, and cells were stained for the early endosomal marker EEA1. (nih.gov)
  • TBC1D9B functions as a GTPase-activating protein for Rab11a in polarized MDCK cells. (nih.gov)
  • F) Top, full-length flag-TBC1D9B-WT or flag-TBC1D9B-RYQ/AAA was immunoprecipitated from HeLa cell lysates and a GAP assay performed using Rab11a or Rab8a loaded with [γ-32P]GTP and incubated for 60 min at 30°C. Lysates from nontransfected cells were used as controls. (nih.gov)
  • see Figure 9A later in this article), which is consistent with previous reports that the Rab11a-SN mutant remains membrane bound in MDCK cells (Wang et al. (nih.gov)
  • In contrast, in HEK cells, there was a significant redistribution of Rab11a from recycling endosomes to the cytosol when TBC1D9B-WT, but not when the inactive mutant TBC1D9B-RYQ/AAA, was expressed (Supplemental Figure S2, A and B). This is the expected result for HEK cells if the GDP-bound form of Rab11a increased as a result of expressing TBC1D9B-WT. (nih.gov)
  • Previously, it was shown that NR2C/F transcription factors bind to TCAGGG variant repeats and contribute to telomere maintenance in ALT cells. (bioportfolio.com)
  • This motif is sufficient to target green fluorescent protein (GFP) to cilia of ciliated cells and targets GFP to lipid rafts if the cells are not ciliated. (nih.gov)
  • To test this, live CTS-GFP-expressing cells were labeled with fluorescent cholera toxin B (Fig. 2 B). Cholera toxin B binds GM1 gangliosides and is a marker for membrane domains enriched in these lipids. (nih.gov)
  • In nonciliated cells, there is strong colocalization between the CTS-GFP spots and the cholera toxin-binding sites (Fig. 2 B, a). (nih.gov)
  • 2004). To determine whether the interaction between Na/K-ATPase and Cav1 plays a role in regulating caveolar vesicle trafficking, we first performed fluorescence resonance energy transfer (FRET) analysis to test whether these two proteins have the potential to directly interact in live cells. (nih.gov)
  • A) Cells were transfected with vectors encoding mycRab24wt or mycRab24(D123I) and 24 h later the expressed proteins were localized by immunofluorescence microscopy, using primary antibodies against the myc epitope or the Rab24 C-terminal hypervariable domain, as indicated above each panel. (nih.gov)
  • B) Cells were transfected with a vector encoding Rab24(D123I) without the myc epitope, and the expressed protein was localized with the Rab24 antibody. (nih.gov)
  • D) Transfected cells expressing mycRab24wt or mycRab24(D123I) were lysed in high-detergent buffer (see Methods) and the proteins recovered in the detergent-soluble and insoluble fractions were assayed by SDS-PAGE and immunoblot analysis, using the anti-myc monoclonal antibody. (nih.gov)
  • Rab38 is a member of the Rab small G protein family and is mainly expressed in lung alveolar type II cells and melanocytes. (creative-biogene.com)
  • The bimolecular fluorescence complementation (BiFC) assay results suggest that, in the SNARE-deficient sso2-1 Δsso1 cells, Mso1p, a Sec1p binding protein, helps to target Sec1p(1-657) lacking the C-terminal tail to the sites of secretion. (nih.gov)
  • Specificity
  • Understanding system-level contributions of Rab proteins to evolutionary history provides insight into the multiple processes sculpting cellular transport pathways and the exciting challenges that we face in delving further into the origins of membrane trafficking specificity. (nih.gov)
  • Insights into the RNA quadruplex binding specificity of DDX21. (bioportfolio.com)
  • Interactions
  • hence, their role remains unclear.For many Rabs, this revealed specific interactions with Drosophila orthologs of known effectors.In addition, we found numerous Rab-specific interactions with known components of membrane traffic as well as with diverse proteins not previously linked to organelles or having no known function. (nih.gov)
  • A total of five RabSF regions and four RabF regions have been described, and these correspond to surface loops involved in protein-protein interactions. (nih.gov)
  • Guanine quadruplexes can form in both DNA and RNA and influence many biological processes through various protein interactions. (bioportfolio.com)
  • Family
  • However, most of the members of the protein family even in plants have not been functionally well characterized. (deepdyve.com)
  • Activation of Arp2/3 complex occurs upon binding of an activator in the WASP family of proteins (Millard et al. (nih.gov)
  • Several attributes distinguish this protein from other members of the Rab family, including a low intrinsic GTPase activity. (nih.gov)
  • The Sec1/Munc18 protein family members perform an essential, albeit poorly understood, function in association with soluble n-ethylmaleimide sensitive factor adaptor protein receptor (SNARE) complexes in membrane fusion. (nih.gov)
  • Phosphorylation of two small GTP-binding proteins of the rab family by p34 cdc2. (springer.com)
  • vacuoles
  • Vacuole tethering, docking, and fusion proteins assemble into a "vertex ring" around the apposed membranes of tethered vacuoles before catalyzing fusion. (nih.gov)
  • Toll-Like Rec
  • In mechanistic studies, cholesterol loading of macrophage plasma membranes (cyclodextrin-cholesterol) or endosomal system (AcLDL+U18666A or Npc1 null mutation) activated Toll-like receptor (TLR) signaling, leading to sustained phosphorylation of p38 mitogen-activated protein kinase and induction of p38 targets, including Ctsk, S100a8, Mmp8, and Mmp14. (umassmed.edu)
  • complex
  • Rab4 Interacts with a Second Form of the GARP Complex(A) Proteins isolated from cell lysates ranked by S score for interaction with GST-Rab4 (detergent-free, lighter gray). (nih.gov)
  • Multiple domain insertions and losses in the evolution of the Rab prenylation complex. (nih.gov)
  • Components of this complex display domain insertions relative to paralogous proteins.We characterize in detail the domain structure of all these components and the phylogenetic relationships between the individual domains.We found different domain insertions in different taxa, in alpha-subunits of RGGTase and REP. (nih.gov)
  • This is catalysed by a complex of a catalytic heterodimer (Rab Geranylgeranyl Transferase - RabGGTase) and an accessory protein (Rab Escort Protein. (nih.gov)
  • REP). Components of this complex display domain insertions relative to paralogous proteins. (nih.gov)
  • We profiled the domain architecture of the components of the Rab prenylation complex in evolution. (nih.gov)
  • The results suggest that the Mso1p C terminus is important for Sec1p(1-657) targeting.The BiFC results suggest that Mso1p acts in close association with Sec4p on intracellular membranes in the bud.Our results reveal a novel binding mode between the Sec1p C-terminal tail and the SNARE complex, and suggest a role for Mso1p as an effector of Sec4p. (nih.gov)
  • The results show that the Sec1p tail binds preferentially ternary Sso1p-Sec9p-Snc2p complexes and it enhances ternary SNARE complex formation in vitro. (nih.gov)
  • Our results reveal a novel binding mode between the Sec1p C-terminal tail and the SNARE complex, and suggest a role for Mso1p as an effector of Sec4p. (nih.gov)
  • Protein motors, such as kinesin and myosin, use chemical energy in the form of ATP to physically move along filaments and perform complex mechanical tasks in the cell, such as intracellular transport, cell division and muscle contraction. (dartmouth.edu)
  • Membrane fusion is also catalyzed by a complex protein and lipid machinery that assembles at specific membrane domains. (nih.gov)
  • Rabs
  • Note that many Rabs, for example Rab11, participate extensively in transport routes and hence the localization of this protein is quite extensive. (nih.gov)
  • Rab8, but not several other Rabs implicated in ciliary assembly, binds to the CTS in a coimmunoprecipitation assay. (nih.gov)
  • vitro
  • Although at least one in vitro system can process and methylate the prenylated C-terminal, in an in vitro system that normally express Rab-38 and in vivo the prenylated C-terminal is not proteolytically processed and not methylated. (genecards.org)
  • We show that, in addition to Sec1p, Mso1p can bind the Rab-GTPase Sec4p in vitro. (nih.gov)
  • Rab 5 controls early endosome fusion in vitro. (springer.com)
  • antibody
  • The cytosol and particulate fractions were subjected to SDS-PAGE and immunoblot analysis, using the anti-myc monoclonal antibody to detect the expressed proteins. (nih.gov)
  • mediates
  • Their structure comprises two domains: domain I include the Rab binding platform, whereas domain II in REP mediates binding to the alpha-subunit of RGGTase [29, (nih.gov)