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1 n homologue, and Sec4p, a vesicle-associated Rab protein.
2 re found to cofractionate with the exogenous rab protein.
3 th each specific step mediated by a distinct Rab protein.
4 to the same melanocyte/platelet subfamily of Rab proteins.
5 king of CXCR2 is differentially regulated by Rab proteins.
6  membrane at steady state and interacts with Rab proteins.
7 aracteristics that distinguish it from other Rab proteins.
8 y occurring in ras proteins but not in other rab proteins.
9 cmt-/- cells lacked the ability to methylate Rab proteins.
10 ng events, which were regulated by different Rab proteins.
11 nzyme that attaches geranylgeranyl groups to Rab proteins.
12 at Vps9p recognizes sequence variation among Rab proteins.
13 strated that GDI-1 can operate with multiple Rab proteins.
14 selective interaction of GDI with individual Rab proteins.
15  Little is known about GEFs and GAPs for Ypt/Rab proteins.
16 roups to both cysteines at the C-terminus of Rab proteins.
17 al factor in the evolution of this subset of Rab proteins.
18 ates guanine nucleotide exchange on ARF1 and Rab proteins.
19 aradigm for studies on the mode of action of Rab proteins.
20 ggests that it may be specific for endosomal Rab proteins.
21 is to play a critical role in the binding of Rab proteins.
22 ylated alanine-rich C kinase substrate), and Rab proteins.
23 esearch on biological processes that involve Rab proteins.
24 RabGGTase) is responsible for prenylation of Rab proteins.
25 hat binds to prenylated inactive (GDP-bound) Rab proteins.
26 Gdi), which is involved in the activation of Rab proteins.
27 s to lysosomes by modulating the activity of Rab proteins.
28 the Golgi membrane through interactions with Rab proteins.
29 constitutively active forms of 31 Drosophila Rab proteins.
30  control the activity of membrane-associated Rab proteins.
31  and constitutively active forms of selected Rab proteins.
32 emporally regulated expression of Drosophila Rab proteins.
33  rab33b, the most commonly studied cisternal rab proteins.
34 icantly different in conformation from other Rab proteins.
35 b and does not interact with mono-prenylated Rab proteins.
36 and 14-3-3 proteins but not between ExoS and Rabs proteins.
37 fied as a prenylation-dependent receptor for Rab proteins, also interacts with Ha-Ras, RhoA, TC21, an
38 ablishes a specific interaction between each Rab protein and its effectors.
39 nd for vesicle fusion at the PVC (the Vps21p rab protein and Vps45p SM (Sec1/Munc18) protein) are req
40 ces are highly homologous to other mammalian Rab proteins and also share homology with proteins of th
41         However, it has been unclear whether Rab proteins and effectors are sufficient for intermembr
42           The effects of ethanol exposure on rab proteins and Golgi function are discussed.
43 s of this protein family negatively regulate RAB proteins and modulate the signaling between RABs and
44 onal genetic data, the results indicate that Rab proteins and PI4P collaborate in the association of
45 f a stable complex between newly synthesized Rab proteins and Rab escort protein (REP).
46  has the ability to physically interact with Rab proteins and the nature of this interaction has led
47 ved to establish domains that contain unique Rab proteins and their cognate effectors, which drive al
48                                              Rab proteins and their effectors facilitate vesicular tr
49 enesis, the subcellular localization of some Rab proteins, and comparisons of the localization of wil
50 entified annexins, annexin-binding proteins, Rab proteins, and other proteins involved in membrane or
51          Yip1p function requires Rab-GDI and Rab proteins, and several mutations that abrogate Yip1p
52                A possible mechanism by which Rab proteins are digeranylgeranylated is suggested by th
53                                   While most Rab proteins are equally expressed in polarized and nonp
54                                              Rab proteins are geranylgeranylated on one or two C-term
55                                              Rab proteins are GTPases that cycle between an inactive
56                                Although some Rab proteins are implicated in vesicle and organelle tra
57 icle budding from the donor compartment, Ypt/rab proteins are involved in the targeting of vesicles t
58 GppNHp, structural features common to active Rab proteins are observed.
59                              The majority of Rab proteins are posttranslationally modified with two g
60                                  All nascent Rab proteins are prenylated by geranylgeranyltransferase
61                                              Rab proteins are Ras-related small GTPases that are dige
62  unclear how the expression and functions of Rab proteins are regulated in response to extracellular
63                                              Rab proteins are small GTP-binding proteins that form th
64                                              Rab proteins are small GTPases that are essential elemen
65                                              Rab proteins are small GTPases that play important roles
66                                              Rab proteins are small molecular weight GTPases that con
67                                              Rab proteins are thought to cycle on and off vesicle mem
68                          Activated GTP-bound Rab proteins are thought to interact with effectors to e
69 nhibits the membrane localization of Rho and Rab proteins at statin doses as low as 200 nm, without a
70                                              Rab proteins attach to membranes along the secretory pat
71  that several Ras-related proteins in brain (Rab) proteins become associated to phagosomes, little is
72                               The cycling of Rab proteins between cytosol and intracellular membranes
73 nhibitor (GDI), which regulates the cycle of Rab proteins between membrane and cytosol, forms an incr
74 with the binding of Rab1B revealed that both Rab proteins bind preferentially to their respective res
75 ve, because the nucleotide-free forms of six Rab proteins bind with similar low efficiency to three S
76     This represents the first structure of a Rab protein bound to GDP.
77 change on ARF1 and on members of the related Rab proteins, but not on other small GTP binding protein
78 hanism for regulation of the GTPase cycle of Rab proteins by GDI proteins.
79            Posttranslational modification of Rab proteins by geranylgeranyltransferase type II requir
80  successive addition of two prenyl groups to Rab proteins by the homologous enzyme geranylgeranyltran
81        Together, our data demonstrate that a rab protein can bind directly to a specific cargo protei
82                  Therefore, animal and fungi Rab proteins can be grouped in "Rab functional groups" a
83 ecific interactions of Myo5B with individual Rab proteins can lead to specificity in the regulation o
84                       A glutamine residue of Rab proteins (cis-glutamine) that is essential for intri
85                                              Rab proteins constitute a second group of substrates tha
86                                              Rab proteins constitute the largest branch of the Ras GT
87                                              Rab proteins cycle between inactive and active states as
88                             Here, we examine Rab protein distributions during Drosophila epithelial t
89 nal homologs of the Saccharomyces cerevisiae Rab protein encoded by YPT1 and are differentially expre
90         Here, we systematically analyzed the Rab protein family and found 14 of them (Rab3A/B/C/D, Ra
91  and ability to bind multiple members of the Rab protein family.
92                                              Rab proteins form a nidus for the assembly of multiprote
93 d protein factor that can release prenylated Rab proteins from GDI.
94 g protein activity that regulates removal of Rab proteins from membranes.
95 t in Rab prenylation and REP cannot retrieve Rab proteins from the membranes.
96      Yop1p could also be coprecipitated with Rab proteins from total cellular lysates.
97                         Moreover, individual Rab proteins function at specific sites within the cell,
98 he functional impact of this modification on RAB proteins has not been actively explored.
99                                  A number of Rab proteins have been implicated in cancer development
100   Recent studies of the functions of certain Rab proteins have revealed specific roles in mediating d
101                  Small GTP-binding proteins (rab proteins) have recently been implicated in the regul
102 he classification of 30 out of 31 C. elegans Rab proteins identified here including Rab31/Rab50, a li
103 tor (GEF) that activates a subsequent acting Rab protein in a given pathway; this process has been te
104 of how GDI can be displaced efficiently from Rab protein in order to allow the necessary recruitment
105 along microtubules or actin, the role of any Rab protein in platelet biogenesis is unknown.
106 s the capability to physically interact with Rab proteins in a promiscuous manner; however, a genetic
107                           To bind membranes, Rab proteins in fungal and animal cells must be isopreny
108 nd khc function, we determined Khc-dependent Rab proteins in glia and present evidence that Neurexin
109                                              Rab proteins in mammalian cells, or Ypt1p and Sec4p in y
110              However, by localizing specific Rab proteins in Paramecium cells, we found that paralogu
111 eal a redundant role for two tissue-specific Rab proteins in regulating transport to a tissue-specifi
112  a key role for the Rab38/Rab32 subfamily of Rab proteins in the biogenesis of melanosomes and potent
113 b-specific regions were used to identify new Rab proteins in the databases and suggest rules for nome
114 tide exchange factors (GEFs) for a subset of Rab proteins in the secretory pathway.
115 ith Golgi membranes that binds to prenylated Rab proteins in their GTP-bound state.
116    We have investigated the possible role of Rab proteins in this delivery process, and found Rab27b
117 olgi, suggesting a possible function for Ypt/rab proteins in vesicle budding as well.
118 d the GTPase activity of several other yeast Rab proteins including Ypt1p, Ypt7p, and Ypt51p but show
119 , little is known about how these phagosomal Rab proteins influence phagosome maturation.
120                                              Rab proteins influence vesicle trafficking pathways thro
121              In their active GTP-bound form, Rab proteins interact with proteins termed effector mole
122 ated by studying alpha1B-adrenergic receptor-Rab protein interactions, using Forster resonance energy
123 4 depletion occurs by segregation of the two Rab proteins into discrete domains that can separate.
124 ing for proteins that interact with Rab38, a Rab protein involved in the biogenesis of melanosomes an
125 ructed an activated allele of VPS21, a yeast Rab protein involved in vacuolar protein sorting, and de
126 of Vps21p, and Ypt7p, which is another yeast Rab protein involved in vacuolar protein transport.
127 pathogen-occupied vacuole by focusing on the Rab proteins involved in biogenesis and maintenance of t
128 to and from thylakoids, similar to cytosolic Rab proteins involved in vesicle transport.
129  reveals that only a small pool of recycling Rab protein is essential for growth, and that the rates
130  that the double prenylation modification of Rab proteins is an important feature in the function of
131 fully understood how segregation of cargo or Rab proteins is maintained along the continuous endosoma
132 at there is a specific lipid requirement for Rab protein localization and function.
133 onservation and low redundancy of Drosophila Rab proteins make these transgenic lines a useful tool k
134                The dynamic redistribution of Rab proteins markedly decreased the Rab27A concentration
135 ization of internalized GPRC6A with selected Rab protein markers.
136             In light of recent evidence that rab proteins may act by promoting the stabilization of S
137            To fulfill their function, active Rab proteins need to localize to intracellular membranes
138 nd of membrane transport requires a cycle of Rab protein nucleotide binding and hydrolysis.
139            One gene, rab30 codes for a novel rab protein of 203 amino acids with minimal homology to
140 escribe a collaboration between two distinct Rab-protein-orchestrated trafficking circuits in bladder
141         Here, we tested the possibility that Rab protein overexpression might also have beneficial ef
142 d enhanced green fluorescent protein--tagged Rab proteins, pharmacological protein kinase C activatio
143                                              Rab proteins play a crucial role in the trafficking of i
144                                              Rab proteins play an essential role in vesicle-mediated
145 ation-dependent expression suggest that this Rab protein plays a role in regulating the delivery of f
146  and scutellar bristle development to screen Rab proteins predicted to be substrates for ICMT (ste14
147  fusion event most likely involves SNARE and Rab proteins present on zymogen granules and cellular me
148        We have now determined that a related Rab protein, Rab10, can interact with myosin Va, myosin
149 Under the same conditions two other exocytic rab proteins, rab2 and rab8, remained membrane bound, an
150 factors including myosin Va and at least one Rab protein, Rab27a.
151  machinery interacts with cell type-specific Rab proteins, Rab38 and Rab32, to facilitate transport t
152                                    Among >40 rab proteins, rab38 has a unique COOH terminus which wou
153            Here we report that the endosomal Rab protein Rab4 orchestrates a GTPase cascade that resu
154 e of the extensively studied cisternal Golgi rab protein, rab6, is modulation of Golgi apparatus resp
155 an skin fibroblasts overexpressing endosomal Rab proteins (Rab7 or Rab9) showed a correction in the s
156                                              Rab proteins regulate polarized trafficking to the cell
157                                              Rab proteins regulate vesicular trafficking pathways, be
158             These findings indicate that the Rab protein regulator, AS160, stabilizes ENaC in a regul
159 everse step by stimulating GTP turnover of a Rab protein required for vesicle tethering/docking/fusio
160 -based sequence alignment of Rab9 with other Rab proteins reveals that its active site consists of re
161   These results indicate that an alternative Rab protein satisfies the Ypt1p requirement in Uso1p-dep
162                                              Rab proteins Sec4 and Ypt11, receptors for essential tra
163 ctional upstream membrane traffic, activated rab protein Sec4p, and its guanine exchange factor Sec2p
164 ocyst complex and downstream effector of the rab protein Sec4p, in various mutants.
165  terminus encodes an exchange factor for the Rab protein Sec4p.
166 membrane in yeast requires the function of a Rab protein, Sec4p, and a set of v- and t-SNAREs, the Sn
167         Localization of adenoviral expressed Rab protein showed wild type Rab3D localized to zymogen
168 An equivalent Rab3A mutant (Rab3A[N135I]), a Rab protein specifically involved in regulated secretion
169                     Biochemical screening of Rab protein substrates for RUTBC2 revealed highest GAP a
170              Biochemical screening of RUTBC1 Rab protein substrates revealed highest in vitro GTP hyd
171 -complexed Rab3, and interacts with no other Rab protein tested.
172                                    Among the Rab proteins tested, we found that besides the previousl
173                  REP binds preferentially to Rab proteins that are in the GDP state, but the specific
174  vivo is exclusively confined to a subset of Rab proteins that are localized to the Golgi apparatus.
175 plexes represent a pool of active, recycling Rab proteins that can deliver Rabs to specific and disti
176 reted reporter protein, we have searched for Rab proteins that function in exocytosis.
177 CK) epithelial cells, belongs to a family of Rab proteins that includes Rab8 and Rab13.
178                As is the case for most other rab proteins, the precise molecular interactions by whic
179                                  A subset of Rab proteins, the Rab3 proteins are thought to play an i
180  release of GDI, and the membrane-associated Rab protein then exchanges its bound GDP for GTP.
181 itive factor attachment protein receptor and Rab proteins to "tether" vacuolar membranes before fusio
182 uble geranyl-geranyl groups are required for Rab proteins to correctly localize to their characterist
183                     The targeting of various Rab proteins to different subcellular compartments appea
184 t Yip1p may function in the process by which Rab proteins translocate between cytosol and membranes.
185                                The PEGylated Rab proteins undergo normal prenylation, underlining the
186 at some of the effector domains can bind two Rab proteins via separate binding sites.
187            Membrane fusion also required the rab protein Vps21p.
188  the regulated cell line AtT-20, this tagged rab protein was found to colocalize with ACTH-containing
189 ermine whether the distribution of secretory rab proteins was altered by ethanol.
190 ntracellular trafficking of FVIIa, EPCR, and Rab proteins was evaluated by immunofluorescence confoca
191 , and the transport steps regulated by these rab proteins were unaffected.
192 acilitates posttranslational modification of Rab proteins, which regulate intracellular trafficking i
193                       Differing from Ras and Rab proteins, which require Mg(2+) for GDP and GTP bindi
194 ntain tightly localized domains of activated Rab proteins, which then serve to recruit other effector
195                        The limited number of Rab proteins with defective membrane association in gm/g
196 rmed by the association of newly synthesized Rab proteins with Rab-escort-protein (REP), the choroide
197                    The data suggest that the Rab protein Ypt1p transiently interacts with the t-SNARE
198 nteracts genetically and physically with the Rab protein Ypt1p, intra-Golgi SNARE molecules, as well
199  SNAREs Bos1p, Sec22p, Bet1p, Sed5p, and the Rab protein, Ypt1p, are distributed similarly but locali
200 nd biochemical tests revealed that a related Rab protein, Ypt6, might substitute for Ypt1p in ypt1Del

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