Results 281 to 290 of about 154,453 (348)

Regulation of vesicular transport by GTP-binding proteins

Current Opinion in Nephrology and Hypertension, 1995
Intracellular protein trafficking occurs in a series of transport vesicles. Vesicle trafficking is regulated both by heterotrimeric and monomeric GTP-binding proteins (G proteins). Recent studies have explored effector systems used by heterotrimeric G proteins and by monomeric ADP-ribosylation factor G proteins for regulation of vesicle budding.
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Overexpression of developmentally regulated GTP-binding protein-2 increases bone loss

American Journal of Physiology-Endocrinology and Metabolism, 2013
The developmentally regulated GTP-binding protein-2 (DRG2) is a novel subclass of GTP-binding proteins. Many functional characteristics of osteoclasts (OC) are associated with small GTPases. We hypothesized that DRG2 affects bone mass via modulating OC activity. Using DRG2 transgenic mice, we investigated the role of DRG2 in bone remodeling.
Ke, Ke, Ok-Joo, Sul, Woon-Ki, Kim, Mi-Hyun, Lee, Myung-Seok, Ko, Jae-Hee, Suh, Hyun-Ju, Kim, Shin-Yoon, Kim, Jeong-Woo, Park, Hye-Seon, Choi   +9 more
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Regulation of phospholipase D by low molecular weight GTP-binding proteins

Journal of Lipid Mediators and Cell Signalling, 1996
Phospholipase D (PLD) is believed to play an important role in cell signal transduction: PLD catalyzes the hydrolysis primarily of phosphatidylcholine (PC) to produce phosphatidic acid that may serve as a lipid second messenger. Although the mechanism of PLD activation has not yet been fully understood, a member of the low molecular weight GTP-binding ...
Y, Kanaho, T, Yokozeki, H, Kuribara
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Rab3 Small GTP—Binding Proteins: Regulation by Calcium/Calmodulin

2003
Rab proteins, forming a subfamily of 52 predominantly membrane-bound, low molecular weight GTP-binding proteins (G-proteins) of the Ras superfamily, are involved in vesicle traffic between intracellular organelles, endocytosis and exocytosis, and may be regulated by calcium (Ca2 +) and/or calmodulin (CaM).
Ranjinder S. Sidhu, Richard R. Clough, Rajinder P. Bhullar   +2 more
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Regulation of G protein-coupled receptor endocytosis by ARF6 GTP-binding proteins

Biochemistry and Cell Biology, 2004
The function of G protein-coupled receptors is regulated by a broad variety of membrane-bound and intracellular proteins. These act in concert to activate signaling pathways that will lead to the desensitization of activated receptors and, for most receptor types, their trafficking to intracellular compartments.
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Distribution and Regulation of RAB3C, a Small Molecular Weight GTP-Binding Protein

Biochemical and Biophysical Research Communications, 1994
We have investigated the expression and regulation of rab3C in rat tissues and rat pheochromocytoma PC12 cells by using a polyclonal antibody that specifically recognizes this protein. Rab3C was expressed in the neuroendocrine systems, as is its highly homologous family member, rab3A.
Y C, Su, L S, Kao, Y Y, Chu, Y, Liang, M H, Tsai, Y, Chern   +5 more
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The regulation of mitochondrial physiology by organelle‐associated GTP‐binding proteins

Cell Biochemistry and Function, 2002
AbstractRecent studies have shown that GTP‐binding proteins can modulate mitochondrial membrane fusion and fission. Furthermore, GTP‐binding proteins can regulate the binding of ribosomes to the mitochondrial membrane and may facilitate the import of proteins through contact points between inner and outer mitochondrial membranes.
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Characterization of DRGs, developmentally regulated GTP-binding proteins, from pea and Arabidopsis

Plant Molecular Biology, 1999
Developmentally regulated GTP-binding proteins (DRGs) from animals and fungi are highly conserved but have no known function. Here we characterize DRGs from pea (PsDRG) and Arabidopsis (AtDRG). Amino acid sequences of AtDRG and PsDRG were 90% identical to each other and about 65% identical to human DRG.
M L, Devitt, K J, Maas, J P, Stafstrom
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Regulation of phagocyte function by low molecular weight GTP‐binding proteins

European Journal of Haematology, 1993
Abstract:  The mechanisms used by phagocytic leukocytes in the process of bacterial killing are regulated by GTP‐binding proteins of the Ras superfamily. In particular, the formation of toxic oxygen metabolites via the NADPH oxidase requires the action of both Rac and Rap1A proteins.
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Low molecular weight GTP-binding proteins: molecular switches regulating diverse cellular functions

American Journal of Physiology-Gastrointestinal and Liver Physiology, 1994
Low molecular weight GTP-binding proteins (LMWG proteins) form a family of proteins that shows homology with Ras, are 18-30 kDa in mass, and bind and hydrolyze GTP. They act as molecular switches, being active when binding GTP. Their activity is regulated by other proteins that influence the dissociation of GDP and the rate of GTP hydrolysis.
A C, Wagner, J A, Williams
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