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Entamoeba histolytica
Published in Dongyou Liu, Handbook of Foodborne Diseases, 2018
Jesús Serrano-Luna, Moisés Martínez-Castillo, Nidia Leon-Sicairos, Mineko Shibayama, Mireya de la Garza
The complex relationship between host cells, gut microbiota, pathogenic bacteria, and E. histolytica is governed by inherent signaling systems, which play important roles in the infection progress30; for example, they have direct implications for parasite migration, proliferation, differentiation, locomotion, and metabolism.6,31 Many aspects of amoeba signaling have been found to be regulated by Ca2+, and diverse calcium proteins have been found in E. histolytica. The EhCaBP1 and EhCaBP3 are involved in actin bundling, which regulates parasite adhesion, phagocytosis, and proliferation,32–35 while URE3-BP and calmodulin have a direct effect in its virulence.36,37 The rearrangement of the actin cytoskeleton that participates in adhesion, motility, tissue invasion, and phagocytosis has been found to be regulated by heterotrimeric G-proteins. The role of Rab proteins has been widely studied in terms of intracellular signaling; these proteins are part of the Rho and Rac families.38–41
Individual conditions grouped according to the international nosology and classification of genetic skeletal disorders*
Published in Christine M Hall, Amaka C Offiah, Francesca Forzano, Mario Lituania, Michelle Fink, Deborah Krakow, Fetal and Perinatal Skeletal Dysplasias, 2012
Christine M Hall, Amaka C Offiah, Francesca Forzano, Mario Lituania, Michelle Fink, Deborah Krakow
Genetics: an autosomal recessive condition caused by mutations of the gene RAB23; Rab proteins belong to the Ras superfamily and are small GTPases involved in the regulation of intracellular membrane trafficking. RAB23 has been demonstrated to negatively regulate the sonic hedgehog signalling pathway.
The rab Gene Family
Published in Juan Carlos Lacal, Frank McCormick, The ras Superfamily of GTPases, 2017
Armand Tavitian, Ahmed Zahraoui
Three lines of evidence show that rab proteins are involved in the regulation of several steps of exocytic and endocytic pathways. Rab proteins share much higher similarity with YPT1p and SEC4p, particularly in the region known as the putative effector domain, than with other ras-like GTP-binding proteins. The raMA gene can complement YPT1 deletions in S. cerevisiae.4 This suggests that rabps, YPT1p, and SEC4p can interact with related effectors and, thus, exert related functions. In agreement with this, it has been shown that a peptide with two substitutions (rab3AL) corresponding to the effector domain of rab3Ap blocks ER to Golgi and intra-Golgi transport in vitro.53rab proteins share highly variable C terminal domains that specify their localization in appropriate secretory compartments.54 Many rab proteins have been localized, they have been found in distinct subcompartments along the exocytic and endocytic pathways (Figure 3). rabl Ap is associated with ER and/or Golgi structures49 (B. Goud personal communication). rab2p is localized in the intermediate compartment between ER and Golgi, rabóp is associated with eis, medial, and especially with trans-Golgi and rab3Ap is present on synaptic vesicles and chromaffin granules. Three other rab proteins are found on endocytic organelles: rab4p and rab5p are associated with PM and early endosomes and rab7p with late endosomes.55-59Recently, direct lines of evidence have shown that rab proteins control vesicle transport. Using an assay which reconstitutes transport between the ER and the cis-Golgi compartment, Plutner et al.60 have shown that rablBp is required in an initial step in export of protein from the ER. It is also required for protein transport between cis- and medial Golgi cisternae. rab5p is needed for the fusion of early endosomes, as was demonstrated by the use of specific antibodies to rab5p in a cell-free assay. Conversely, fusion of endosomes is stimulated by an excess of wild-type rab5p.61 It was shown that rab3Ap dissociates from synaptic vesicle fraction after calcium-dependent exocytosis in synaptosomes, and that this dissociation is partially reversible during recovery after stimulation.62 These results show an association-dissociation cycle of rab3Ap during exocytosis.
Lithium effects on vesicular trafficking in hepatocellular carcinoma cells
Published in Ultrastructural Pathology, 2019
Iuliia Taskaeva, Nataliya Bgatova, Izabella Gogaeva
Endosomal transport pathways are closely associated with receptor signaling and the Ras-associated binding protein family of small GTPases involved in endocytic trafficking.5 Rab proteins constitute a family of small GTP-binding proteins which localize in distinct intracellular compartments and regulate diverse endocytotic events.6 Endocytotic markers can be detected in different endosomal compartments, such as early, late and recycling endosomes. Early endosome antigen 1 (EEA1) localizes to early endosomes and is associated with endosome fusion7,8 while Ras-related protein 7 (Rab7) has been found in late endosomes and is implicated in transport from early to late endocytic compartments.6 Ras-related protein 11 (Rab11) participates in the endocytic recycling and regulation of transport from early and recycling endosomes to the cell surface and has been detected in recycling endosomes.5,9
Rab11-mediated recycling endosome role in nervous system development and neurodegenerative diseases
Published in International Journal of Neuroscience, 2021
Jiajia Zhang, Gang Su, Qionghui Wu, Jifei Liu, Ye Tian, Xiaoyan Liu, Juanping Zhou, Juan Gao, Wei Chen, Deyi Chen, Zhenchang Zhang
Small Rab proteins belong to the Ras superfamily GTPases and consist of approximately 70 different proteins. Rab GTPases can participate in the stage of secretory and endocytic vesicular traffic by coordinating with effector, such as budding of the donor membrane, vesicular trafficking, and docking fusion of vesicles to the acceptor membrane [1, 2]. Rab11, as a critical member of the Rab family, consists of Rab11a, Rab11b and Rab11c/Rab25 [3]. Rab11 is mainly localized to the Golgi apparatus, endosomes, and vesicles derived from endocytosis and exocytosis [4], and mediates endosome recycling to trans-Golgi network (TGN) and plasma membrane by endosome recovery chamber/recycling endosome (ERC/RE) in intracellular vesicle traffic [5] (Figure 1).
Relationship between the effect of polyunsaturated fatty acids (PUFAs) on brain plasticity and the improvement on cognition and behavior in individuals with autism spectrum disorder
Published in Nutritional Neuroscience, 2022
Isabel Barón-Mendoza, Aliesha González-Arenas
Vesicle trafficking is mainly regulated by SNARE (Soluble NSF Attachment Protein) proteins [131]. SNARE proteins are at vesicle membranes (v-SNAREs) as in target membranes (t-SNAREs). v-SNARE and t-SNARE pairing promotes the fusion of membranes by using the energy released during the formation of a trans-SNARE complex, which consists of a four α helix beam that allows the narrow approaching of membranes for the beginning of the fusion [132]. The specificity of this fusion mechanism is supported by the vesicle addressing to the target membrane by Rab proteins. Rab proteins are monomeric GTPases, which in its GTP-bound active state guide a vesicle to a specific target membrane for its following fusion [133].