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1 n homologue, and Sec4p, a vesicle-associated Rab protein.
2 th each specific step mediated by a distinct Rab protein.
3 re found to cofractionate with the exogenous rab protein.
4 signaling by specifically dephosphorylating Rab proteins.
5 b and does not interact with mono-prenylated Rab proteins.
6 to the same melanocyte/platelet subfamily of Rab proteins.
7 king of CXCR2 is differentially regulated by Rab proteins.
8 membrane at steady state and interacts with Rab proteins.
9 aracteristics that distinguish it from other Rab proteins.
10 y occurring in ras proteins but not in other rab proteins.
11 cmt-/- cells lacked the ability to methylate Rab proteins.
12 nzyme that attaches geranylgeranyl groups to Rab proteins.
13 at Vps9p recognizes sequence variation among Rab proteins.
14 strated that GDI-1 can operate with multiple Rab proteins.
15 selective interaction of GDI with individual Rab proteins.
16 Little is known about GEFs and GAPs for Ypt/Rab proteins.
17 roups to both cysteines at the C-terminus of Rab proteins.
18 al factor in the evolution of this subset of Rab proteins.
19 ates guanine nucleotide exchange on ARF1 and Rab proteins.
20 aradigm for studies on the mode of action of Rab proteins.
21 ggests that it may be specific for endosomal Rab proteins.
22 is to play a critical role in the binding of Rab proteins.
23 , which selectively dephosphorylates phospho-Rab proteins.
24 th the MHC-I complex and endosome-associated RAB proteins.
25 mutation result, but may connect to NET via RAB proteins.
26 ng events, which were regulated by different Rab proteins.
27 ylated alanine-rich C kinase substrate), and Rab proteins.
28 esearch on biological processes that involve Rab proteins.
29 ignaling by controlling dephosphorylation of Rab proteins.
30 RabGGTase) is responsible for prenylation of Rab proteins.
31 hat binds to prenylated inactive (GDP-bound) Rab proteins.
32 Gdi), which is involved in the activation of Rab proteins.
33 s to lysosomes by modulating the activity of Rab proteins.
34 the Golgi membrane through interactions with Rab proteins.
35 constitutively active forms of 31 Drosophila Rab proteins.
36 control the activity of membrane-associated Rab proteins.
37 and constitutively active forms of selected Rab proteins.
38 emporally regulated expression of Drosophila Rab proteins.
39 rab33b, the most commonly studied cisternal rab proteins.
40 icantly different in conformation from other Rab proteins.
41 and 14-3-3 proteins but not between ExoS and Rabs proteins.
42 eveloped highly sensitive sensors to monitor Rab protein activity in single dendritic spines undergoi
44 fied as a prenylation-dependent receptor for Rab proteins, also interacts with Ha-Ras, RhoA, TC21, an
46 nd for vesicle fusion at the PVC (the Vps21p rab protein and Vps45p SM (Sec1/Munc18) protein) are req
47 ces are highly homologous to other mammalian Rab proteins and also share homology with proteins of th
50 NOTCH4-dependent transcriptional control of RAB proteins and intracellular vesicle trafficking in au
51 P1), which is responsible for prenylation of Rab proteins and is essential for intracellular traffick
52 s of this protein family negatively regulate RAB proteins and modulate the signaling between RABs and
53 onal genetic data, the results indicate that Rab proteins and PI4P collaborate in the association of
55 has the ability to physically interact with Rab proteins and the nature of this interaction has led
56 ved to establish domains that contain unique Rab proteins and their cognate effectors, which drive al
58 enesis, the subcellular localization of some Rab proteins, and comparisons of the localization of wil
59 entified annexins, annexin-binding proteins, Rab proteins, and other proteins involved in membrane or
60 ty of LRRK2 to associate with phosphorylated Rab proteins, and phosphorylated Rab8A stimulates LRRK2
68 icle budding from the donor compartment, Ypt/rab proteins are involved in the targeting of vesicles t
73 unclear how the expression and functions of Rab proteins are regulated in response to extracellular
80 small hydrolase enzymes (or GTPases) called Rab proteins, arranged on the cytoplasmic surface of its
81 nhibits the membrane localization of Rho and Rab proteins at statin doses as low as 200 nm, without a
84 that several Ras-related proteins in brain (Rab) proteins become associated to phagosomes, little is
86 nhibitor (GDI), which regulates the cycle of Rab proteins between membrane and cytosol, forms an incr
87 with the binding of Rab1B revealed that both Rab proteins bind preferentially to their respective res
88 ve, because the nucleotide-free forms of six Rab proteins bind with similar low efficiency to three S
90 change on ARF1 and on members of the related Rab proteins, but not on other small GTP binding protein
93 successive addition of two prenyl groups to Rab proteins by the homologous enzyme geranylgeranyltran
96 ecific interactions of Myo5B with individual Rab proteins can lead to specificity in the regulation o
100 e experiments indicate that Golgi-associated Rab proteins contribute to the localization of PPM1H, an
103 nal homologs of the Saccharomyces cerevisiae Rab protein encoded by YPT1 and are differentially expre
117 Recent studies of the functions of certain Rab proteins have revealed specific roles in mediating d
119 he classification of 30 out of 31 C. elegans Rab proteins identified here including Rab31/Rab50, a li
120 tor (GEF) that activates a subsequent acting Rab protein in a given pathway; this process has been te
121 of how GDI can be displaced efficiently from Rab protein in order to allow the necessary recruitment
123 s the capability to physically interact with Rab proteins in a promiscuous manner; however, a genetic
126 nd khc function, we determined Khc-dependent Rab proteins in glia and present evidence that Neurexin
129 eal a redundant role for two tissue-specific Rab proteins in regulating transport to a tissue-specifi
130 a key role for the Rab38/Rab32 subfamily of Rab proteins in the biogenesis of melanosomes and potent
131 b-specific regions were used to identify new Rab proteins in the databases and suggest rules for nome
134 We have investigated the possible role of Rab proteins in this delivery process, and found Rab27b
136 d the GTPase activity of several other yeast Rab proteins including Ypt1p, Ypt7p, and Ypt51p but show
140 ated by studying alpha1B-adrenergic receptor-Rab protein interactions, using Forster resonance energy
141 4 depletion occurs by segregation of the two Rab proteins into discrete domains that can separate.
142 ing for proteins that interact with Rab38, a Rab protein involved in the biogenesis of melanosomes an
143 ructed an activated allele of VPS21, a yeast Rab protein involved in vacuolar protein sorting, and de
144 of Vps21p, and Ypt7p, which is another yeast Rab protein involved in vacuolar protein transport.
145 pathogen-occupied vacuole by focusing on the Rab proteins involved in biogenesis and maintenance of t
146 ecent studies have revealed that a subset of RAB proteins involved in secretory and endocytic recycli
148 reveals that only a small pool of recycling Rab protein is essential for growth, and that the rates
149 that the double prenylation modification of Rab proteins is an important feature in the function of
150 fully understood how segregation of cargo or Rab proteins is maintained along the continuous endosoma
152 onservation and low redundancy of Drosophila Rab proteins make these transgenic lines a useful tool k
159 escribe a collaboration between two distinct Rab-protein-orchestrated trafficking circuits in bladder
161 d enhanced green fluorescent protein--tagged Rab proteins, pharmacological protein kinase C activatio
165 ation-dependent expression suggest that this Rab protein plays a role in regulating the delivery of f
166 and scutellar bristle development to screen Rab proteins predicted to be substrates for ICMT (ste14
167 fusion event most likely involves SNARE and Rab proteins present on zymogen granules and cellular me
169 Under the same conditions two other exocytic rab proteins, rab2 and rab8, remained membrane bound, an
171 machinery interacts with cell type-specific Rab proteins, Rab38 and Rab32, to facilitate transport t
174 e of the extensively studied cisternal Golgi rab protein, rab6, is modulation of Golgi apparatus resp
175 an skin fibroblasts overexpressing endosomal Rab proteins (Rab7 or Rab9) showed a correction in the s
179 everse step by stimulating GTP turnover of a Rab protein required for vesicle tethering/docking/fusio
180 -based sequence alignment of Rab9 with other Rab proteins reveals that its active site consists of re
181 These results indicate that an alternative Rab protein satisfies the Ypt1p requirement in Uso1p-dep
183 reported effectors of the secretory vesicle Rab protein Sec4, including the myosin-V Myo2, the exocy
185 ctional upstream membrane traffic, activated rab protein Sec4p, and its guanine exchange factor Sec2p
188 membrane in yeast requires the function of a Rab protein, Sec4p, and a set of v- and t-SNAREs, the Sn
190 An equivalent Rab3A mutant (Rab3A[N135I]), a Rab protein specifically involved in regulated secretion
198 vivo is exclusively confined to a subset of Rab proteins that are localized to the Golgi apparatus.
199 plexes represent a pool of active, recycling Rab proteins that can deliver Rabs to specific and disti
206 affinity to endogenous, LRRK2-phosphorylated Rab proteins, thereby blocking dephosphorylation seen up
207 itive factor attachment protein receptor and Rab proteins to "tether" vacuolar membranes before fusio
208 uble geranyl-geranyl groups are required for Rab proteins to correctly localize to their characterist
210 t Yip1p may function in the process by which Rab proteins translocate between cytosol and membranes.
212 In this study, siRNA-based screening of Rab proteins using HBV-expressing cells showed that Rab5
216 the regulated cell line AtT-20, this tagged rab protein was found to colocalize with ACTH-containing
218 ntracellular trafficking of FVIIa, EPCR, and Rab proteins was evaluated by immunofluorescence confoca
220 short interfering RNA (siRNA) screening for Rab proteins, which are considered to act as molecular s
221 acilitates posttranslational modification of Rab proteins, which regulate intracellular trafficking i
223 ntain tightly localized domains of activated Rab proteins, which then serve to recruit other effector
225 rmed by the association of newly synthesized Rab proteins with Rab-escort-protein (REP), the choroide
227 nteracts genetically and physically with the Rab protein Ypt1p, intra-Golgi SNARE molecules, as well
228 SNAREs Bos1p, Sec22p, Bet1p, Sed5p, and the Rab protein, Ypt1p, are distributed similarly but locali
229 nd biochemical tests revealed that a related Rab protein, Ypt6, might substitute for Ypt1p in ypt1Del