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Topic: GTPase superfamily

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	GTPase (Site not responding. Last check: 2007-10-31)
		Throwing the switch is performed by the unidirectional change of the GTPase from the active, GTP -bound form to the inactive, GDP -bound form by hydrolysis of the GTP through intrinsic GTPase-activity, effectively switching the GTPase off.
		It can be reverted (switching the GTPase on again) by Guanine nucleotide exchange factor s (GEFs), which cause the GDP to dissociate from the GTPase, leading to its association with a new GTP.
		Among the target molecules of the active GTPase are adenylate cyclase and ion channel s.
	www.serebella.com /encyclopedia/article-GTPase.html (897 words)

	GTPase - Wikipedia, the free encyclopedia
		Throwing the switch is performed by the unidirectional change of the GTPase from the active, GTP-bound form to the inactive, GDP-bound form by hydrolysis of the GTP through intrinsic GTPase-activity, effectively switching the GTPase off.
		It can be reverted (switching the GTPase on again) by Guanine nucleotide exchange factors (GEFs), which cause the GDP to dissociate from the GTPase, leading to its association with a new GTP.
		Among the target molecules of the active GTPase are adenylate cyclase and ion channels.
	en.wikipedia.org /wiki/GTPase (869 words)

	Small GTPase Superfamily
		Members of the superfamily share approx 30% amino acid sequence identity, with the bulk of this identity derived from four highly conserved domains required for the recognition of GDP, GTP and for GTPase activity.
		The small GTPase superfamily is synonymous with the Ras superfamily, this latter name derived from the Ras protein, the first member of the superfamily to be described.
		The switch is activated by the exchange of GDP for GTP, catalyzed by guanine nucleotide exchange factors (GEFs), in response to a variety of upstream signal signals.
	www.horizonpress.com /gateway/small-gtpase-superfamily.html (337 words)

	GTPase (Site not responding. Last check: 2007-10-31)
		Throwing the switch is performed by the unidirectional change ofthe GTPase from the active, GTP -bound form to the inactive, GDP -bound form by hydrolysis of the GTP through intrinsic GTPase-activity, effectively switching the GTPase off.
		This closes the cycle to the active state of the GTPase; the irreversiblehydrolysis of the GTP to GDP forces the cycle to run only in one direction.
		Among the target molecules of the active GTPase are adenylate cyclase and ionchannels.
	www.therfcc.org /gtpase-108988.html (795 words)

	Targeting Proteins to Membranes
		Their structure provides the molecular basis for a model of protein-targeting to biological membranes in which the formation of the complex is coupled to its subsequent disassembly, thereby insuring that the targeting brings the protein to the membrane but does not remove it (the targeting is unidirectional).
		The SRP and SR proteins are known to be closely related GTPases that belong to the SRP-GTPase family, and their biological role in protein targeting is conserved across all the kingdoms of life.
		However, in contrast to most other members of the GTPase superfamily, activation of the SRP family GTPases is triggered by heterodimer formation between the two homologous GTPase domains in which the G domain and the amino terminal N domain of each are structurally and functionally coupled in an arrangement universally conserved between all SRP-GTPases.
	www-als.lbl.gov /als/science/sci_archive/82protein_membrane.html (1084 words)

	GTPase --Biotechnology Encyclopedia (Site not responding. Last check: 2007-10-31)
		GTPase superfamily, are GTPases used for regulation of other
		Guanine nucleotide exchange factors (GEFs), which cause the GDP to dissociate from the GTPase, leading to its association with a new GTP.
		Among the target molecules of the active GTPase are
	www.biotech100.com /biotechnology_encyclopedia/gtpase.htm (650 words)

	FACULTY ::: Division of Chemistry and Chemical Engineering ::: CALTECH
		A thermodynamic and kinetic framework for the GTPase cycles of SRP and SR.
		Blue and yellow coloring indicate α-helices and β-strands in the SRP GTPase; the corresponding structures in SR are shown in green and pink.
		The results show that during the SRP-SR interaction, both GTPases undergo a series of discrete conformational rearrangements that culminate in the activation of GTP hydrolysis from both proteins (Figure 4).
	www.cce.caltech.edu /faculty/shan/research.html (907 words)

	[Full text] PIKE GTPase Signaling and Function
		GTPases are typically activated by GAP proteins, but whether the Arf-GAP domain functions as an internal GAP for the GTPase activity of PIKE-L remains to be determined, though there are instances of Arf-GAP domains exerting such activity [27].
		The GTPase domain of AGAP1 is 51% similar and 27% identical to K-Ras, AGAP2 is 42% similar and 28% identical to Rab9, and M-RIP is 47% similar and 27% identical to H-Ras [35].
		Phosphoinositide lipids bind to PH domain and activate dynamin GTPase activity, which is important in dynamin function during vesicle budding [36].
	www.biolsci.org /v01p0044.htm (4931 words)

	Regulation of G Protein Activation and Effector Modulation by Fusion Proteins between the Human 5-Hydroxytryptamine1A ...
		Basal high-affinity GTPase activity in membranes of untreated (filled columns) or pertussis toxin treated (hatched columns) cells and its regulation by a range of ligands (all at 100 µM) was assessed for fusion proteins between the human 5HT
		The potency of 5-HT to stimulate high-affinity GTPase activity was assessed in membranes of untreated (open symbols) and pertussis toxin-treated (filled symbols) cells stably expressing the isolated 5-HT -receptor (circles) and fusion proteins with either wild-type (squares) or pertussis toxin-resistant (Gly
		Data are presented as the percentage of the effect produced by 100 µM 5-HT in untreated cells expressing each form of the receptor.
	molpharm.aspetjournals.org /cgi/content/full/56/4/684 (4988 words)

	GTPase
		Signal transduction at the intracellular domain of transmembrane receptorss, including recognition of taste, smell and light.
		The amount of active GTPase can be changed in several ways :
		Brought to you by NoChildLeftBehind.com and the Beaches and Towns Network, LLC.
	www.teachtime.com /en/wikipedia/g/gt/gtpase.html (839 words)

	Peter Walter
		Second, SRP and its receptor are regulated by GTPase switches, which makes possible signal sequence loading in the cytosol and unloading at the membrane.
		The current goal is to decipher how the GTPases are regulated and how the energy of GTP hydrolysis is used in the protein-targeting reaction, possibly to promote fidelity and unidirectionality.
		Recently obtained structures demonstrate that the SRP and SRP receptor GTPases belong to a novel subgroup in the GTPase superfamily.
	www.hhmi.org /research/investigators/walter.html (1719 words)

	Primal de Lanerolle, Ph.D.
		Myosin I and II are members of a superfamily of actin-activated molecular motors that convert chemical energy into mechanical work.
		The actin-myosin II interaction in smooth muscle and non-muscle cells is regulated by the phosphorylation of ser 19 of the 20 kDa light chain of myosin II by the calcium-calmodulin dependent enzyme myosin light chain kinase (MLCK).
		Therefore, we proposed the hypothesis that the level of myosin II light chain phosphorylation is important in determining the integrated cellular response to GTPase activation.
	www.uic.edu /depts/mcpb/pages/primal/primal.htm (966 words)

	Evidence from sequence information that the interleukin-1 receptor is a transmembrane GTPase -- HOPP 4 (9): 1851 -- ...
		superfamily, despite a lack of significant detectable sequence homology.
		segments of the GTPases, it became apparent that the IL-1Rs possess a
		GTPase, then its activation function may be directed to as-yet unrecognized
	www.proteinscience.org /cgi/content/abstract/4/9/1851 (359 words)

	BioMed Central \| Full text \| Mutant Rab24 GTPase is targeted to nuclear inclusions
		Rab proteins comprise a large family of Ras-related GTPases that function in the anterograde and retrograde trafficking of proteins in mammalian cells [1-3].
		When overexpressed in cultured cells, these mutant GTPases function as dominant-suppressors of their endogenous counterparts [26,27,31], presumably because they can compete for interaction with effectors, exchange factors or docking proteins, but cannot cycle on and off membranes in a nucleotide-dependent manner.
		Although the formation of intranuclear inclusions has not been observed in previous studies of Ras-related GTPases, it is a common feature of several neurodegenerative disorders where abnormal proteins containing poly-Gln tracts are synthesized as a result of CAG codon expansions [52].
	www.biomedcentral.com /1471-2121/3/25 (7307 words)

	WHAT ARE THE MECHANISMS OF PHOTORECEPTOR ADAPTATION?
		Ting and Ho (1991) report GTPase activity more rapid than PDE inactivation, but do not prove that the burst of GTPase activity observed in their experiments is associated with transducin, nor do they measure GTPase and PDE inactivation under the same conditions.
		The rates of Gt GTPase and PDE turnoff measured in the same suspension of bovine ROS coincide (Arshavsky et al., 1989; Angleson and Wensel, 1993).
		GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase.
	www.bbsonline.org /documents/a/00/00/04/35/bbs00000435-00/bbs.neur3.bownds.html (11479 words)

	EMBL - Research - Structural and Computational Biology Unit - Scheffzek Team
		GTPase activating proteins: structural and functional insights 18 years after discovery.
		Human Lsg1 defines a family of essential GTPases that correlates with the evolution of compartmentalization.
		Evolutionary relationship between the bacterial HPr kinase and the ubiquitous PEP-carboxykinase: expanding the P-loop nucleotidyl transferase superfamily.
	www-db.embl-heidelberg.de /jss/emblGroups/per_1061.html (997 words)

	Anti-SARI, SARI, SARI antibody
		SAR1 protein belongs to the small GTPase superfamily, SAR1 family.
		It is involved in transport from the endoplasmic reticulum to the Golgi apparatus (by similarity).
		Jones, B. et al : Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders.
	www.prosci-inc.com /Antibody-XW-TDS/XW-7549.html (79 words)

	UCSF's Frank McCormick: A Multidisciplinary Focus on Cancer
		His 1991 Nature paper on the GTPase superfamily has over 1,300 citations alone (see the table on the next page).
		In looking for what could be missing, we discovered in cellular extracts that there is a factor that would massively accelerate the GTP hydrolysis on normal ras by thousands of fold but which had no effect on the mutant protein.
		We called that factor GAP for GTPase Activating Protein, because it had the property of accelerating GTP hydrolysis rates of the ras protein.
	www.sciencewatch.com /nov-dec98/sw_nov-dec98_page3.htm (1265 words)

	Yi Zheng, PhD, Cincinnati Children's Hospital Medical Center (Site not responding. Last check: 2007-10-31)
		The Rho family small GTP-binding proteins of Ras superfamily, including Rho, Rac, and Cdc42, are a class of intracellular signal transducers that play important roles in the regulation of cell growth and actin-based morphogenesis.
		Elucidation of the mechanisms underlying the molecular interactions between individual Rho family GTPases and their regulatory/effector proteins, with goals to gain insight to the mechanisms of regulation of the Rho proteins and to address the issue how the signals bifurcate at the small GTP-binding proteins to cause diverse cellular responses.
		The goals are to dissect the molecular pathways of Rho GTPases that cooperate with p53 deficiency in promoting cell transformation and invasion and to implicate individual members of the Rho family as anti-cancer targets in the p53 deficient onco-mouse model.
	www.cincinnatichildrens.org /svc/find-professional/z/yi-zheng.htm (1986 words)

	Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates -- Meier ... (Site not responding. Last check: 2007-10-31)
		Era GTPase of Escherichia coli: binding to 16S rRNA and modulation of GTPase activity by RNA and carbohydrates -- Meier et al.
		GTPase activities of the purified GST–Era and native Era proteins of E.
		Ingram, G. C., Simon, R., Carpenter, R. and Coen, E. The Antirrhinum ERG gene encodes a protein related to bacterial small GTPases and is required for embryonic viability.
	mic.sgmjournals.org /cgi/content/full/146/5/1071 (6039 words)

	Pfam 20.0 : RhoGEF (Site not responding. Last check: 2007-10-31)
		Activation of Rho proteins through release of bound GDP and subsequent binding of GTP, is catalyzed by guanine nucleotide exchange factors (GEFs) in the Dbl family.
		Biochemical data have established the role of the conserved DH domain in Rho GTPase interaction and activation, and the role of the tandem PH domain in intracellular targeting and/or regulation of DH domain function.
		The DH domain is composed of 11 alpha helices that are folded into a flattened, elongated alpha-helix bundle in which two of the three conserved regions, conserved region 1 (CR1) and conserved region 3 (CR3), are exposed near the center of one surface.
	pfam.wustl.edu /cgi-bin/getdesc?acc=PF00621 (511 words)

	Intra- and Intermolecular Domain Interactions of the C-terminal GTPase Effector Domain of the Multimeric Dynamin-like ...
		Drp1 is a member of the dynamin superfamily of multimeric large
		of the mammalian Drp1 GTPase, focusing on the role of the C-terminal
		The GTPase activity of wild-type Drp1 is abolished by the K38A mutation and markedly diminished by the K679A mutation.
	www.jbc.org /cgi/content/full/279/34/35967 (4714 words)

	Small GTPase - Term Explanation on IndexSuche.Com (Site not responding. Last check: 2007-10-31)
		This family of proteins are homologous to Ras GTPases and also called the Ras superfamily GTPases.
		Small GTPases regulate a wide variety of processes in the cell, including growth, cellular_differentiation, cell movement and lipid vesicle transport.
		Small GTPases hydrolyse GTP quickly when they are bound to GTPase-activating protein (GAP), and slowly when they are not bound to GAP.
	www.indexsuche.com /Small_GTPase.html (254 words)

	Douglas M. Freymann, PhD
		The SRP GTPases are structurally similar to other well-known members of the GTPase superfamily, such as Ras, Ran, and the Ga subunits of the heterotrimeric G-proteins.
		The structures of the SRP GTPases Ffh and FtsY have suggested new mechanisms by which function can be elaborated from a common GTPase fold.
		Our laboratory is now focusing on understanding the structural basis for regulation of the two SRP GTPases, using high resolution X-ray crystallographic studies of the nucleotide-bound Ffh (Ramirez, 2006) and biochemical, biophysical and crystallographic studies of the assembly of the Ffh:FtsY targeting complex (Focia, 2006; Gawronski-Salerno, 2006).
	www.feinberg.northwestern.edu /igp/facindex/FreymannD.html (504 words)

	Genome Biology \| Full text \| The septins
		Of the five conserved motifs found in other members of the GTPase superfamily, three are highly conserved in septins.
		The GTPase motifs of the septins are closer to those of the Ras family than of other members of the GTPase superfamily [6] such as the other cytoskeletal GTPases, tubulins in eukaryotes or FtsZ in bacteria.
		The G-1 motif (which has a consensus in the superfamily of GxxxxGK[S/T] in the single-letter amino-acid code) is well conserved, and the consensus around the G-1 motif of septins is GESGLGKSTLINTLF (where the bold residues are strictly conserved).
	www.genomebiology.com /2003/4/11/236 (4500 words)

	Superfamily (biology) (Site not responding. Last check: 2007-10-31)
		In biology a superfamily is an intermediate taxonomic rank between suborder and family.
		A number of genera may be grouped into a family.
		What words can be used to fully describe and convey the awesome genius that is Curtis Mayfield's Superfly album, one of the Must Own records of soul?Having led The Impressions for a decade, Curtis stepped into his solo career with two incredible albums, 1...
	www.freeglossary.com /Superfamily_(biology) (213 words)

	The Superfamily of Rho GTPase-Activating Proteins (Site not responding. Last check: 2007-10-31)
		GTP hydrolysis is a key step in many intracellular processes.
		GTPases are the molecular machines that catalyze this reaction but their intrinsic GTPase activity is very slow in the case of the Ras superfamily of GTPases.
		This hydrolysis can be accelerated by orders of magnitude upon interaction with GTPase-activating proteins (GAPs), which are specific for their respective GTP-binding proteins.
	www.eurekah.com /abstract.php?chapid=1327&bookid=104&catid=56 (211 words)

	Evidence that Dynamin-2 Functions as a Signal-transducing GTPase -- Fish et al. 150 (1): 145 -- The Journal of Cell ...
		The GTPase dynamin binds to and is activated by a subset of SH3 domains.
		Lin, H.C., and Gilman, A.G. Regulation of dynamin I GTPase activity by G protein betagamma subunits and phosphatidylinositol 4,5 bisphosphate.
		Warnock, D.E., Terlecky, L.J., and Schmid, S.L. Dynamin GTPase is stimulated by crosslinking through the C terminal proline rich domain.
	www.jcb.org /cgi/content/full/150/1/145 (5829 words)

	UCSF's Frank McCormick: A Multidiscipinary Focus on Cancer
		Our idea was to develop research programs in each of those areas and identify drug targets, screen them ourselves initially or, as we became more savvy, set up research collaborations with pharmaceutical companies where we would provide the protein targets and they would do the high-throughput screening.
		H.R. Bourne, D.A. Sanders, F. McCormick, "The GTPase superfamily: Conserved structure and molecular mechanism," Nature, 349(6305):117-27, 1991.
		H.R. Bourne, D.A. Sanders, F. McCormick, "The GTPase superfamily: a conserved switch for diverse cell functions," Nature, 348(6297):125-32, 1990.
	www.sciencewatch.com /nov-dec98/sw_nov-dec98_page4.htm (1294 words)

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