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Dielle E Whitecross et al.
Scientific reports, 7(1), 16194-16194 (2017-11-25)
Rab5 is a small monomeric GTPase that mediates protein trafficking during endocytosis. Inactivation of Rab5 by GTP hydrolysis causes a conformational change that masks binding sites on its "switch regions" from downstream effectors. The p85 subunit of phosphatidylinositol 3-kinase (PI3K)
Zhu Li et al.
The Journal of biological chemistry, 292(10), 3977-3987 (2017-01-29)
IcmF is a 5'-deoxyadenosylcobalamin (AdoCbl)-dependent enzyme that catalyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA. It is a bifunctional protein resulting from the fusion of a G-protein chaperone with GTPase activity and the cofactor- and substrate-binding mutase domains with
Bryan A Tornabene et al.
Protein science : a publication of the Protein Society, 29(6), 1416-1428 (2020-01-26)
Dynamin-superfamily proteins (DSPs) are large self-assembling mechanochemical GTPases that harness GTP hydrolysis to drive membrane remodeling events needed for many cellular processes. Mutation to alanine of a fully conserved lysine within the P-loop of the DSP GTPase domain results in
Identification of the binding surface on Cdc42Hs for p21-activated kinase.
Guo W, Sutcliffe MJ, et al.
Biochemistry, 37, 14030-14037 (1988)
GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2
Biosa A, et al.
Human Molecular Genetics, 22(6), 1140-1156 (2012)
Michal P Wandel et al.
Nature immunology, 21(8), 880-891 (2020-06-17)
Bacterial lipopolysaccharide triggers human caspase-4 (murine caspase-11) to cleave gasdermin-D and induce pyroptotic cell death. How lipopolysaccharide sequestered in the membranes of cytosol-invading bacteria activates caspases remains unknown. Here we show that in interferon-γ-stimulated cells guanylate-binding proteins (GBPs) assemble on
Sandro F Ataide et al.
Science (New York, N.Y.), 331(6019), 881-886 (2011-02-19)
Cotranslational targeting of membrane and secretory proteins is mediated by the universally conserved signal recognition particle (SRP). Together with its receptor (SR), SRP mediates the guanine triphosphate (GTP)-dependent delivery of translating ribosomes bearing signal sequences to translocons on the target
Joshua S Chappie et al.
Cell, 147(1), 209-222 (2011-10-04)
The GTPase dynamin catalyzes membrane fission by forming a collar around the necks of clathrin-coated pits, but the specific structural interactions and conformational changes that drive this process remain a mystery. We present the GMPPCP-bound structures of the truncated human
Ravi Kiran Koripella et al.
Nature communications, 11(1), 3830-3830 (2020-08-02)
The mammalian mitochondrial ribosome (mitoribosome) and its associated translational factors have evolved to accommodate greater participation of proteins in mitochondrial translation. Here we present the 2.68-3.96 Å cryo-EM structures of the human 55S mitoribosome in complex with the human mitochondrial elongation
Emmanuel Derivery et al.
Nature, 528(7581), 280-285 (2015-12-15)
During asymmetric division, fate determinants at the cell cortex segregate unequally into the two daughter cells. It has recently been shown that Sara (Smad anchor for receptor activation) signalling endosomes in the cytoplasm also segregate asymmetrically during asymmetric division. Biased
Gilles Labesse et al.
Nucleic acids research, 39(8), 3458-3472 (2010-12-15)
Nucleoside Monophosphate Kinases (NMPKs) family are key enzymes in nucleotide metabolism. Bacterial UMPKs depart from the main superfamily of NMPKs. Having no eukaryotic counterparts they represent attractive therapeutic targets. They are regulated by GTP and UTP, while showing different mechanisms
Catarina da Silveira Tomé et al.
The FEBS journal, 285(1), 160-177 (2017-11-18)
EngA is a conserved bacterial GTPase involved in ribosome biogenesis. While essential in bacteria, EngA does not have any human orthologue and can thus be an interesting target for new antibacterial compounds. EngA is the only known GTPase bearing two
Structural inhibition of dynamin-mediated membrane fission by endophilin
Hohendahl A, et al.
eLife, 6, e26856-e26856 (2017)
Jean-Marc Taymans et al.
PloS one, 6(8), e23207-e23207 (2011-08-23)
Leucine rich repeat kinase 2 (LRRK2) is a Parkinson's disease (PD) gene that encodes a large multidomain protein including both a GTPase and a kinase domain. GTPases often regulate kinases within signal transduction cascades, where GTPases act as molecular switches
T Schweins et al.
Journal of molecular biology, 266(4), 847-856 (1997-03-07)
GTP and ATP hydrolysing proteins have an absolute requirement for a divalent cation, which is usually Mg2+, as a cofactor in the enzymatic reaction. Other phosphoryl transfer enzymes employ more than one divalent ion for the enzymatic reaction. It is
T S Lai et al.
The Journal of biological chemistry, 273(3), 1776-1781 (1998-01-27)
Tissue transglutaminase (tTG) catalyzes a Ca(2+)-dependent transglutaminase (TGase) activity that stabilizes tissues and a GTP hydrolysis activity that regulates cell receptor signaling. The purpose of this study was to examine the true substrates for nucleotide hydrolysis and the effects of
Veronica R Moorman et al.
Journal of molecular biology, 426(21), 3520-3538 (2014-08-12)
Human cell division cycle protein 42 (Cdc42Hs) is a small, Rho-type guanosine triphosphatase involved in multiple cellular processes through its interactions with downstream effectors. The binding domain of one such effector, the actin cytoskeleton-regulating p21-activated kinase 3, is known as
Lakshmi Srinivasan et al.
Biochimica et biophysica acta, 1858(4), 698-705 (2016-01-18)
Solute carrier (SLC) 26 or sulfate permease (SulP) anion transporters, belong to a phylogenetically ancient family of secondary active transporters. Members of the family are involved in several human genetic diseases and cell physiological processes. Despite their importance, the substrates
Raphael Gasper et al.
Small GTPases, 1(3), 133-141 (2011-06-21)
The Ras family is the largest and most diverse sub-group of Ras-like G proteins. This complexity is further increased by the high number of regulatory Guanine nucleotide Exchange Factors (GEFs) and GTPase Activating Proteins (GAPs) that target specific members of
Joseph Gawronski-Salerno et al.
Journal of structural biology, 158(1), 122-128 (2006-12-23)
Ffh and FtsY are GTPase components of the signal recognition particle co-translational targeting complex that assemble during the SRP cycle to form a GTP-dependent and pseudo twofold symmetric heterodimer. Previously the SRP GTPase heterodimer has been stabilized and purified for
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