Biological Control Activities of Rice-Associated Bacillus sp. Strains against Sheath Blight and Bacterial Panicle Blight of Rice.
The five selected RABs showing highest antimicrobial activities (RAB6, RAB9, RAB16, RAB17S, and RAB18) were closest to B. amyloliquefaciens in DNA sequence of 16S rDNA and gyrB, but to B. subtilis in that of recA.
Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo.
Interestingly, the lysosomal abnormalities in these lrrk mutants can be suppressed by a constitutively active form of the small GTPase rab9, which promotes retromer-dependent recycling from late endosomes to the Golgi.
A fat body-derived apical extracellular matrix enzyme is transported to the tracheal lumen and is required for tube morphogenesis in Drosophila.
This process was defective in rab9 and shrub/vps32 mutants and in wild-type embryos treated with a secretory pathway inhibitor, leading to an abundant accumulation of Serp in the fat body.
The Amyloid Precursor Protein is rapidly transported from the Golgi apparatus to the lysosome and where it is processed into beta-amyloid.
By photoactivating APP-paGFP in the Golgi, using the Golgi marker Galactosyltranferase fused to Cyan Fluorescent Protein (GalT-CFP) as a target, we are able to follow a population of nascent APP molecules from the Golgi to downstream compartments identified with compartment markers tagged with red fluorescent protein (mRFP or mCherry); including rab5 (early endosomes) rab9 (late endosomes) and LAMP1 (lysosomes).
The small GTPases Rab9A and Rab23 function at distinct steps in autophagy during Group A Streptococcus infection.
Rab9A and Rab23 GTPases play crucial roles in autophagy of Group A Streptococcus.
RUTBC2 protein, a Rab9A effector and GTPase-activating protein for Rab36.
These data show that RUTBC2 can act as a Rab36 GAP in cells and suggest that RUTBC2 links Rab9A function to Rab36 function in the endosomal system.
Protein kinase A inhibition modulates the intracellular routing of gene delivery vehicles in HeLa cells, leading to productive transfection.
Rather, we identify a novel compartment, tentatively characterized as a transferrin(-)/rab9(-)/LAMP1(-) compartment, to which cargo within the clathrin-mediated pathway of endocytosis is rerouted upon inhibition of PKA, and which may act as an alternative and effective site of cargo release in gene delivery.
RUTBC1 is a Tre2/Bub2/Cdc16 domain-containing protein that binds to Rab9A-GTP both in vitro and in cultured cells, but is not a GTPase-activating protein for Rab9A.
Involvement of Rab9 and Rab11 in the intracellular trafficking of TRPC6.
Results describe the involvement of two Rab GTPases, Rab9 and Rab11, in the trafficking of TRPC6.
Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9.
Data show that recombinant HPS1-HPS4 produced in insect cells can be efficiently isolated as a 1:1 heterodimer, and might function as a Rab9 effector in the biogenesis of lysosome-related organelles.
Lipid metabolism in cystic fibrosis.
Accumulation of free cholesterol in distinct perinuclear compartments, reversible by overexpression of rab9, suggests that cystic fibrosis and the lysosomal storage disease Niemann-Pick-C could share similar cell signaling defects, in addition to increased cAMP signaling and sterol-regulatory element binding protein (SREBP) expression that affect cholesterol metabolism.
Limited role for SREBP-1c in defective glucose-induced insulin secretion from Zucker diabetic fatty rat islets: a functional and gene profiling analysis.
Rab3), stimulated (voltage-dependent Ca(2+) channel subunit alpha1D, CPT2, SUR2, rab9, syt13), or inhibited (syntaxin 7, secretogranin-2) by SREBP-1c inhibition.
Endocytic trafficking of glycosphingolipids in sphingolipid storage diseases.
Golgi targeting of GSLs internalized via caveolae is dependent on microtubules and phosphoinositide 3-kinase(s) and is inhibited by expression of dominant-negative rab7 and rab9 constructs.
Intracellular membrane trafficking pathways in bone-resorbing osteoclasts revealed by cloning and subcellular localization studies of small GTP-binding rab proteins.
Rab1B, rab4B, rab5C, rab7, rab9, rab11B, and rab35 were identified from rat osteoclasts in this study.
The predicted protein product of the gene consists of 201 amino acid residues, and the protein has 86% similarity to human RAB9 at the amino acid level.
The small GTP binding protein rab7 is essential for cellular vacuolation induced by Helicobacter pylori cytotoxin.
Dominant-negative mutants of rab7 effectively prevented vacuolization, whereas homologous rab5 and rab9 mutants were only partially inhibitory or ineffective, respectively.
METHODS: Cell line from rabbit dermal fibroblasts (RAB9) and primary cultures of rabbit corneal stroma fibroblasts (NRCF) were grown to confluence.
Biochemical analysis of rab9, a ras-like GTPase involved in protein transport from late endosomes to the trans Golgi network.
rab9 is a ras-like GTPase which has been implicated in the transport of mannose 6-phosphate receptors between late endosomes and the trans Golgi network.
Rab GDI: a solubilizing and recycling factor for rab9 protein.
We show here that the cytosolic form of rab9, a protein required for transport between late endosomes and the trans Golgi network, also occurs as a complex with a GDI-like protein, with an apparent mass of approximately 80 kD.
Rab9 functions in transport between late endosomes and the trans Golgi network.
We report here the primary sequence, subcellular localization and functional activity of a new member of the rab protein family, rab9.