Results 1 to 10 of about 43,338 (208)
p21ras and several other ras-related GTP-binding proteins are modified post-translationally by addition of 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenoids to cysteines within a conserved carboxyl-terminal sequence motif, Caa(M/S/L), where a is an aliphatic amino acid.
B. Therese Kinsella, William A. Maltese
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The Human Rab Genes Encode a Family of GTP-binding Proteins Related to Yeast YPT1 and SEC4 Products Involved in Secretion [PDF]
Seven cDNA clones corresponding to the rab1, rab2, rab3A, rab3B, rab4, rab5, and rab6 genes were isolated from a human pheochromocytoma cDNA library. They encode 23-25 kDa polypeptides which share approximately 30-50% homology and belong to the ras superfamily.
Ahmed Zahraoui+3 more
semanticscholar +4 more sources
Rab proteins are a family of Ras-like GTPases involved in intracellular membrane traffic. Rab GDI, a cytosolic protein which inhibits the dissociation of GDP from various Rab proteins, is required to maintain a pool of Rab proteins in the cytosol.
Zvulun Elazar+2 more
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Highly purified lysosomes, prepared by magnetic fractionation of homogenates from Dictyostelium discoideum cells fed colloidal iron, were lysed under hypoosmotic conditions, and the membrane-associated proteins were subjected to gel electrophoresis. Thirteen major membrane polypeptides, ranging in molecular weight from 25,000 to 100,000 were identified.
Lesly A. Temesvari+4 more
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Small GTP binding proteins: Rab GTPases from the brain of Bombyx mori [PDF]
From a mRNA of the brain of Bombyx mori, we isolated 8 cDNA clones (BRabs), each of which encodes a different member of Rab-protein family. Four of them have more than 80% amino acid identity to the corresponding members of Drosophila Rab proteins.
Tomohide Uno, Susumu Hiragaki
semanticscholar +5 more sources
Rab proteins are membrane-bound prenylated GTP-binding proteins required for the targeted movement of membrane vesicles from one organelle to another. In the current paper we have characterized and purified an enzyme that attaches geranylgeranyl residues to Rab proteins that bear the COOH-terminal sequence Cys-X-Cys (such as Rab3A) and Cys-Cys (such as
Miguel C. Seabra+3 more
semanticscholar +5 more sources
Role of the Rab GTP-Binding Protein Ypt3 in the Fission Yeast Exocytic Pathway and Its Connection to Calcineurin Function [PDF]
A genetic screen for mutations synthetically lethal with fission yeast calcineurin deletion led to the identification of Ypt3, a homolog of mammalian Rab11 GTP-binding protein. A mutant with the temperature-sensitive ypt3-i5 allele showed pleiotropic phenotypes such as defects in cytokinesis, cell wall integrity, and vacuole fusion, and these were ...
Hong Cheng+9 more
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Location of light-repressible, small GTP-binding protein of the YPT/rab family in the growing zone of etiolated pea stems. [PDF]
YPT/rab proteins are ras-like small GTP-binding proteins that serve as key regulators of vesicular transport. The mRNA levels of two YPT/rab genes in pea plants are repressed by light, with the process mediated by phytochrome. Here, we examined the mRNA expression and the location of the two proteins, pra2- and pra3-encoded proteins, using monoclonal ...
Yukio Nagano+4 more
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Identification of small GTP-binding rab proteins in human platelets: thrombin-induced phosphorylation of rab3B, rab6, and rab8 proteins. [PDF]
The activation of platelets by specific agonists is a tightly regulated mechanism that leads to the secretion of the dense- and alpha-granule contents. Platelets have been shown to possess small GTP-binding proteins thought to be involved in central biological processes; however, no rab proteins, which may regulate the exocytic process at different ...
A. Karniguian+2 more
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Low molecular mass GTP-binding proteins encoded by the mammalian rab genes are found in membranes of the Golgi complex and endosomes, suggesting that they play a role in the movement of exocytic and endocytic vesicles. The basis for the membrane association of these proteins has not been defined.
B. Therese Kinsella, William A. Maltese
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