PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24555545-1 2014 Member RAS oncogene family (RAB1A), a member of the RAS oncogene family, cycles between inactive GDP-bound and active GTP-bound forms regulating vesicle transport in exocytosis. Guanosine Triphosphate 118-121 RAB1A, member RAS oncogene family Homo sapiens 28-33 30605611-5 2019 We demonstrate that the switching between GTP and GDP binding states, which is governed by guanine nucleotide exchange factors (GEFs), GTPase-activating proteins (GAPs), GDI, and GDI displacement factor (GDF), is a major determinant of Rab1"s ability to effectively cycle between cellular compartments and eventually its subcellular distribution. Guanosine Triphosphate 42-45 RAB1A, member RAS oncogene family Homo sapiens 236-240 27768524-5 2018 C9orf72 interacts with Rab1a, preferentially in its GTP-bound state, as well as the ULK1 autophagy initiation complex. Guanosine Triphosphate 52-55 RAB1A, member RAS oncogene family Homo sapiens 23-28 26953259-7 2016 However, this variant shows no specificity for GXP nucleotides, a constantly enhanced GTP hydrolysis activity and is no longer controlled by GEF or GAP proteins, indicating a new regulatory mechanism for the Rab1A cycle via alternative non-trivial splicing. Guanosine Triphosphate 86-89 RAB1A, member RAS oncogene family Homo sapiens 208-213 25446900-3 2014 AA stimulates Rab1A GTP binding and interaction with mTORC1 and Rheb-mTORC1 interaction in the Golgi. Guanosine Triphosphate 20-23 RAB1A, member RAS oncogene family Homo sapiens 14-19 15796781-2 2005 Rab1 is thought to act as a molecular switch and can change between an active GTP-bound and an inactive GDP-bound conformation. Guanosine Triphosphate 78-81 RAB1A, member RAS oncogene family Homo sapiens 0-4 20861236-0 2010 Rab1 small GTP-binding protein regulates cell surface trafficking of the human calcium-sensing receptor. Guanosine Triphosphate 11-14 RAB1A, member RAS oncogene family Homo sapiens 0-4 18413237-3 2008 Much is known about the role of Rab1 in ER-to-Golgi trafficking through overexpression of dominant negative mutation that inhibit GTP binding or GTPase activity of the protein, as well as through the use of antibodies to inhibit endogenous protein activity. Guanosine Triphosphate 130-133 RAB1A, member RAS oncogene family Homo sapiens 32-36 23815289-1 2013 Rab proteins are a large family of GTP-binding proteins that regulate cellular membrane traffic and organelle identity. Guanosine Triphosphate 35-38 RAB1A, member RAS oncogene family Homo sapiens 0-3 23382462-5 2013 Here, we demonstrate that Rab-activating guanosine diphosphate/guanosine triphosphate exchange factors (GEFs) display the minimal targeting machinery for recruiting Rabs from the cytosol to the correct membrane using the Rab-GEF pairs Rab5A-Rabex-5, Rab1A-DrrA, and Rab8-Rabin8 as model systems. Guanosine Triphosphate 63-85 RAB1A, member RAS oncogene family Homo sapiens 26-29 23382462-5 2013 Here, we demonstrate that Rab-activating guanosine diphosphate/guanosine triphosphate exchange factors (GEFs) display the minimal targeting machinery for recruiting Rabs from the cytosol to the correct membrane using the Rab-GEF pairs Rab5A-Rabex-5, Rab1A-DrrA, and Rab8-Rabin8 as model systems. Guanosine Triphosphate 63-85 RAB1A, member RAS oncogene family Homo sapiens 250-255 22628317-4 2012 Our results show that GTP-bound Rab1 interacts with the F(x)(6)LL motif of beta2AR. Guanosine Triphosphate 22-25 RAB1A, member RAS oncogene family Homo sapiens 32-36 20861236-2 2010 Here we investigated the role of Rab1, a small GTP-binding protein that specifically regulates protein transport from the endoplasmic reticulum to the Golgi, in cell surface transport of the hCaR. Guanosine Triphosphate 47-50 RAB1A, member RAS oncogene family Homo sapiens 33-37 19942850-1 2010 GDP-bound prenylated Rabs, sequestered by GDI (GDP dissociation inhibitor) in the cytosol, are delivered to destined sub-cellular compartment and subsequently activated by GEFs (guanine nucleotide exchange factors) catalysing GDP-to-GTP exchange. Guanosine Triphosphate 233-236 RAB1A, member RAS oncogene family Homo sapiens 21-25 19361519-2 2009 Here we measured rate and equilibrium constants that define the interaction of Ypt1p with guanine nucleotide (guanosine 5"-diphosphate and guanosine 5"-triphosphate/guanosine 5"-(beta,gamma-imido)triphosphate) and the core TRAPP subunits required for GEF activity. Guanosine Triphosphate 139-164 RAB1A, member RAS oncogene family Homo sapiens 79-84 11718716-3 2001 A GST-rab33b fusion protein stabilised in its GTP form was found to interact by Western blotting or mass spectroscopy with Golgi protein GM130 and rabaptin-5 and rabex-5, two rab effector molecules thought to function exclusively in the endocytic pathway. Guanosine Triphosphate 46-49 RAB1A, member RAS oncogene family Homo sapiens 6-9 12656988-3 2003 Golgin-84 is a membrane-anchored golgin that we now show binds preferentially to the GTP form of the rab1 GTPase. Guanosine Triphosphate 85-88 RAB1A, member RAS oncogene family Homo sapiens 101-105 12221137-5 2002 These findings implicate small GTP-binding proteins of the Ypt/Rab family in a signal cascade that directs membrane traffic through the secretory pathway. Guanosine Triphosphate 31-34 RAB1A, member RAS oncogene family Homo sapiens 63-66 11739401-2 2001 The GTP form of rab1 regulates ER to Golgi transport by interaction with the vesicle tethering factor p115 and the cis-Golgi matrix protein GM130, also part of a complex with GRASP65 important for the organization of cis-Golgi cisternae. Guanosine Triphosphate 4-7 RAB1A, member RAS oncogene family Homo sapiens 16-20 11038176-2 2000 Previous studies have shown that YPT1, which encodes the small GTP-binding protein that regulates membrane traffic at this stage of the secretory pathway, interacts genetically with BET3 and BET5. Guanosine Triphosphate 63-66 RAB1A, member RAS oncogene family Homo sapiens 33-37 11419942-1 2001 The activities of three Rab-specific factors with GDP/GTP exchange activity, Vps9p, Rabex-5 and DSS4, with their cognate GTPases, Ypt51p, Rab5 and Ypt1p, have been analysed quantitatively. Guanosine Triphosphate 54-57 RAB1A, member RAS oncogene family Homo sapiens 147-152 11239471-6 2001 Once the vesicle binds to TRAPP I, the small GTP binding protein Ypt1p is activated and other tethering factors are recruited. Guanosine Triphosphate 45-48 RAB1A, member RAS oncogene family Homo sapiens 65-70 11419942-6 2001 An additional, and based on present knowledge, unique, feature of the Ypt1p.DSS4 complex, is that the association of GTP (or GDP) is more than 10(3)-fold slower than to Ypt1p, thus leading to a long life-time of the binary complex between the two proteins, even at the high nucleotide concentrations that prevail in the cell. Guanosine Triphosphate 117-120 RAB1A, member RAS oncogene family Homo sapiens 70-75 9763446-2 1998 Cycling between the GDP- and GTP-bound forms and the accessory proteins that regulate this cycling are thought to be crucial for Ypt/Rab function. Guanosine Triphosphate 29-32 RAB1A, member RAS oncogene family Homo sapiens 133-136 9763446-6 1998 The Ypt1p-GEF stimulates GDP release and GTP uptake at least 10-fold and is specific for Ypt1p. Guanosine Triphosphate 41-44 RAB1A, member RAS oncogene family Homo sapiens 4-9 9763446-6 1998 The Ypt1p-GEF stimulates GDP release and GTP uptake at least 10-fold and is specific for Ypt1p. Guanosine Triphosphate 41-44 RAB1A, member RAS oncogene family Homo sapiens 89-94 9763446-9 1998 The Ypt1p-GAP stimulates GTP hydrolysis by Ypt1p up to 54-fold, has a higher affinity for the GTP-bound form of Ypt1p than for the GDP-bound form, and is specific to a subgroup of exocytic Ypt proteins. Guanosine Triphosphate 25-28 RAB1A, member RAS oncogene family Homo sapiens 4-9 9763446-9 1998 The Ypt1p-GAP stimulates GTP hydrolysis by Ypt1p up to 54-fold, has a higher affinity for the GTP-bound form of Ypt1p than for the GDP-bound form, and is specific to a subgroup of exocytic Ypt proteins. Guanosine Triphosphate 25-28 RAB1A, member RAS oncogene family Homo sapiens 43-48 9763446-9 1998 The Ypt1p-GAP stimulates GTP hydrolysis by Ypt1p up to 54-fold, has a higher affinity for the GTP-bound form of Ypt1p than for the GDP-bound form, and is specific to a subgroup of exocytic Ypt proteins. Guanosine Triphosphate 25-28 RAB1A, member RAS oncogene family Homo sapiens 43-48 9763446-9 1998 The Ypt1p-GAP stimulates GTP hydrolysis by Ypt1p up to 54-fold, has a higher affinity for the GTP-bound form of Ypt1p than for the GDP-bound form, and is specific to a subgroup of exocytic Ypt proteins. Guanosine Triphosphate 94-97 RAB1A, member RAS oncogene family Homo sapiens 4-9 9763446-9 1998 The Ypt1p-GAP stimulates GTP hydrolysis by Ypt1p up to 54-fold, has a higher affinity for the GTP-bound form of Ypt1p than for the GDP-bound form, and is specific to a subgroup of exocytic Ypt proteins. Guanosine Triphosphate 94-97 RAB1A, member RAS oncogene family Homo sapiens 43-48 9763446-9 1998 The Ypt1p-GAP stimulates GTP hydrolysis by Ypt1p up to 54-fold, has a higher affinity for the GTP-bound form of Ypt1p than for the GDP-bound form, and is specific to a subgroup of exocytic Ypt proteins. Guanosine Triphosphate 94-97 RAB1A, member RAS oncogene family Homo sapiens 43-48 9447979-5 1998 To test this idea, we inactivated the GTPase activity of Ypt1p by using the Q67L mutation, which targets a conserved residue that helps catalyze GTP hydrolysis in Ras. Guanosine Triphosphate 38-41 RAB1A, member RAS oncogene family Homo sapiens 57-62 9447979-6 1998 We demonstrate that the mutant Ypt1-Q67L protein is severely impaired in its ability to hydrolyze GTP both in the absence and in the presence of GAP and consequently is restricted mostly to the GTP-bound form. Guanosine Triphosphate 98-101 RAB1A, member RAS oncogene family Homo sapiens 31-35 9447979-6 1998 We demonstrate that the mutant Ypt1-Q67L protein is severely impaired in its ability to hydrolyze GTP both in the absence and in the presence of GAP and consequently is restricted mostly to the GTP-bound form. Guanosine Triphosphate 194-197 RAB1A, member RAS oncogene family Homo sapiens 31-35 9441742-2 1997 Mss4 is a guanine-nucleotide-exchange factor for the Sec4/ Ypt1/Rab family of small GTP-binding proteins involved in the regulation of intracellular vesicular transport. Guanosine Triphosphate 84-87 RAB1A, member RAS oncogene family Homo sapiens 59-63 9441742-2 1997 Mss4 is a guanine-nucleotide-exchange factor for the Sec4/ Ypt1/Rab family of small GTP-binding proteins involved in the regulation of intracellular vesicular transport. Guanosine Triphosphate 84-87 RAB1A, member RAS oncogene family Homo sapiens 64-67 9034329-3 1997 Rab delivery to cellular membranes involves release of GDI, and the membrane-associated Rab protein then exchanges its bound GDP for GTP. Guanosine Triphosphate 133-136 RAB1A, member RAS oncogene family Homo sapiens 0-3 9447979-12 1998 These results suggest that the function of Ypt1p in vesicular transport requires not only the GTP-bound form of the protein but also the interaction of Ypt1p with its GNEF. Guanosine Triphosphate 94-97 RAB1A, member RAS oncogene family Homo sapiens 43-48 7619808-1 1995 The Sec4/Ypt1/Rab family of small GTP-binding proteins are involved in the regulation of intracellular vesicular transport. Guanosine Triphosphate 34-37 RAB1A, member RAS oncogene family Homo sapiens 9-13 8603910-5 1996 In addition, overexpression of the small GTP-binding protein Ypt1p, or of a gain if function mutant (SLY1-20) of the t-SNARE associated protein Sly1p, also confers temperature resistance. Guanosine Triphosphate 41-44 RAB1A, member RAS oncogene family Homo sapiens 61-66 7619808-1 1995 The Sec4/Ypt1/Rab family of small GTP-binding proteins are involved in the regulation of intracellular vesicular transport. Guanosine Triphosphate 34-37 RAB1A, member RAS oncogene family Homo sapiens 14-17 8008830-4 1994 As a step towards positional cloning of the wr gene, we have mapped the locus to proximal chromosome 11, thus excluding CNTF and its receptor as candidates, and suggesting the closely-linked Rab 1 gene encoding a GTP-binding protein as a possibility. Guanosine Triphosphate 213-216 RAB1A, member RAS oncogene family Homo sapiens 191-196 8175881-13 1994 Moreover, BFA recovery is incomplete in the presence of rab1 mutants or GTP gamma S. We conclude that GTP exchange and hydrolysis by GTPases, specifically rab1a, are required to form and maintain normal Golgi stacks. Guanosine Triphosphate 72-75 RAB1A, member RAS oncogene family Homo sapiens 155-160 8175881-13 1994 Moreover, BFA recovery is incomplete in the presence of rab1 mutants or GTP gamma S. We conclude that GTP exchange and hydrolysis by GTPases, specifically rab1a, are required to form and maintain normal Golgi stacks. Guanosine Triphosphate 102-105 RAB1A, member RAS oncogene family Homo sapiens 56-60 8175881-13 1994 Moreover, BFA recovery is incomplete in the presence of rab1 mutants or GTP gamma S. We conclude that GTP exchange and hydrolysis by GTPases, specifically rab1a, are required to form and maintain normal Golgi stacks. Guanosine Triphosphate 102-105 RAB1A, member RAS oncogene family Homo sapiens 155-160 8163542-2 1994 To explore the role of rab1 we have analyzed the function of a mutant (rab1a[S25N]) containing a substitution which perturbs Mg2+ coordination and reduces the affinity for GTP, resulting in a form which is likely to be restricted to the GDP-bound state. Guanosine Triphosphate 172-175 RAB1A, member RAS oncogene family Homo sapiens 71-76 8380507-1 1993 Rab geranylgeranyl transferase (GG transferase) is a two-component enzyme that attaches 20-carbon isoprenoid groups to cysteine residues in Rab proteins, a family of guanosine triphosphate-binding proteins that regulate vesicular traffic. Guanosine Triphosphate 166-188 RAB1A, member RAS oncogene family Homo sapiens 0-3 1447289-15 1992 These results are consistent with the hypothesis that multiple GTP-binding proteins including a heterotrimeric G protein(s), ARF and rab1 differentially regulate steps in the transport of protein between early compartments of the secretory pathway. Guanosine Triphosphate 63-66 RAB1A, member RAS oncogene family Homo sapiens 133-137 1850747-1 1991 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. Guanosine Triphosphate 19-22 RAB1A, member RAS oncogene family Homo sapiens 65-68 1902553-0 1991 Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2. Guanosine Triphosphate 29-32 RAB1A, member RAS oncogene family Homo sapiens 57-60 1902553-6 1991 The GTP-binding proteins of the Rab family in rats and humans display strong homologies with Sec4p and Ypt1p, and might therefore also be involved in regulating intracellular transport. Guanosine Triphosphate 4-7 RAB1A, member RAS oncogene family Homo sapiens 32-35 1902553-6 1991 The GTP-binding proteins of the Rab family in rats and humans display strong homologies with Sec4p and Ypt1p, and might therefore also be involved in regulating intracellular transport. Guanosine Triphosphate 4-7 RAB1A, member RAS oncogene family Homo sapiens 103-108 34453713-5 2021 We found that the switching between GTP- and GDP-binding states, which is governed by guanine nucleotide exchange factors (GEFs), GTPase activating proteins (GAPs), GDP dissociation inhibitor (GDI) and GDI displacement factor (GDF), is a major determinant for Rab1"s ability to effectively cycle between cellular compartments and eventually for its subcellular distribution. Guanosine Triphosphate 36-39 RAB1A, member RAS oncogene family Homo sapiens 260-264 2501306-0 1989 The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. Guanosine Triphosphate 39-42 RAB1A, member RAS oncogene family Homo sapiens 10-13 2501306-7 1989 The homology (approximately 30%) between these rab proteins and p21ras is restricted to the four conserved domains involved in the GTP/GDP binding. Guanosine Triphosphate 131-134 RAB1A, member RAS oncogene family Homo sapiens 47-50 1321151-2 1992 Rab proteins are membrane-bound prenylated GTP-binding proteins required for the targeted movement of membrane vesicles from one organelle to another. Guanosine Triphosphate 43-46 RAB1A, member RAS oncogene family Homo sapiens 0-3 1904626-0 1991 Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1 protein. Guanosine Triphosphate 73-76 RAB1A, member RAS oncogene family Homo sapiens 85-89 1904626-1 1991 The function of the guanosine triphosphate (GTP)-binding protein Ypt1 in regulating vesicular traffic was studied in a cell-free system that reconstitutes transport from the endoplasmic reticulum to the Golgi. Guanosine Triphosphate 20-42 RAB1A, member RAS oncogene family Homo sapiens 65-69 1904626-1 1991 The function of the guanosine triphosphate (GTP)-binding protein Ypt1 in regulating vesicular traffic was studied in a cell-free system that reconstitutes transport from the endoplasmic reticulum to the Golgi. Guanosine Triphosphate 44-47 RAB1A, member RAS oncogene family Homo sapiens 65-69 2115402-5 1990 These findings provide evidence that members of the YPT1/SEC4 subfamily of GTP binding proteins are localized to specific exocytic and endocytic subcompartments in mammalian cells. Guanosine Triphosphate 75-78 RAB1A, member RAS oncogene family Homo sapiens 52-56 1966913-2 1990 In analogy to small GTP-binding proteins like SEC4 to YPT1, it has been suggested that botulinum D toxin substrates might be involved in secretory process of myeloid cells. Guanosine Triphosphate 20-23 RAB1A, member RAS oncogene family Homo sapiens 54-58 32790781-11 2020 The interaction was nucleotide dependent and it was favored with GTP-locked active state variants of these GTPases, indicating that human GOLPH3 is a bona fide effector of RAB1A and RAB1B. Guanosine Triphosphate 65-68 RAB1A, member RAS oncogene family Homo sapiens 172-177