GTPase


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GTPase

[′jē‚tē¦pās]
(cell and molecular biology)
One of a family of monomeric GTP-binding proteins.
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In this research, the authors suggested positive results associated with potential apoptotic and anti-metastatic effects due to endoplasmic reticulum stress, oxidative stress and Rho GTPase signaling pathways.
Seven CpGs that passed Bonferroni-threshold (p < 6.5 x [10.sup.-8]) were located upstream of the ABR (ABR activator of RhoGEF and GTPase) gene on chromosome 17 (cg01912040, cg10003262), in the SEMA4G (semaphorin 4G) gene body on chromosome 10 (cg05962511), in the MAPRE2 (microtubule associated protein RP/EB family member 2) gene body (cg17420142), in the GBAP1 (glucosylceramidase beta pseudogene 1) gene body (cg06466147), in the NSMF gene body (cg09082427), and in the NBR1 (NBR1 autophagy cargo receptor) 5' untranslated region (UTR) (cg04193083).
Previous studies have shown that Grail can regulate expression of CD151 and CD83 through ubiquitin-mediated protein degradation.[5],[6],[7] Moreover, the Rho guanine dissociation inhibitor (RhoGDI) has been shown to be associated with Grail and is capable of mediating T cells activation, which in turn inhibits the RhoA GTPase activity through increasing the stability of the RhoGDI; RhoA GTPase has been shown to regulate the organization of the cytoskeleton and IL-2 expression.[7] Another study demonstrated that the mammalian target of rapamycin (mTOR) pathway mediates cell-cycle progression and proliferation of naive T cell by regulating the expression of Grail.[8] This evidence implies that Grail may play an important role in cell cycle arrest and proliferation.
The ARHGAP1 gene product is a member of the Rho GTPase family known to regulate multiple eukaryotic cell functions including actin cytoskeleton reorganization, polarity establishment, and cell growth.
(6-8) All of these processes are mediated by GTPase proteins, including elongation factors, (9) tubulin, (10) and dynamin family members.
aeruginosa isolates recovered from urinary tract, trachea and wound.22 However, rare production of phospholipase C was observed in vitro by Tielen et al.20 The virulence factor exoS is a bifunctional toxin with both adenosine diphosphate ribosyl transferase (ADPRT) activity and guanosine triphosphate-ase (GTPase) activating protein (GAP) activity.21
One study has shown that the rs3213758 locus in the retinitis pigmentosa GTPase regulator-interacting protein 1-like ( RPGRIP1L )gene might increase the risk of vitiligo in a Korean population.[4] In addition, several mutations in the RPGRIP1L gene were associated with various clinical phenotypes of nervous system diseases.[5] However, the relationship between RPGRIP1L gene polymorphisms and susceptibility to SV in the Chinese Han population has not been reported.
The Rho GTPase proteins have a critical role in cytoskeletal rearrangement, and its activity is altered by EPEC effector proteins (38).
(2005) suggested Ran, a small GTPase, to be involved in contractile ring formation.
For example, the presence of activating KRAS proto-oncogene, GTPase (KRAS) [12]; NRAS proto-oncogene, GTPase (NRAS); and B-Raf proto-oncogene, serine/threonine kinase (BRAF) mutations conveys primary resistance of metastatic colorectal adenocarcinomas to anti-epidermal growth factor receptor (EGFR) antibodies (i.e., cetuximab, panitumumab) (2, 3) and the genetic screening of these mutations is now part of routine practice.
A small GTPase Rab8 participates in cholesterol transport from LE to PM in Myosin5-dependent movement of cholesterolenriched lysosome-related organelles along actin cytoskeleton [82].