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1 COPI and clathrin represent two important and distinct s
2 COPI coated vesicles carry material between Golgi compar
3 COPI coated vesicles mediate trafficking within the Golg
4 COPI in these mutants is released from Golgi membranes b
5 COPI is a coatomer protein complex responsible for intra
6 COPI is required for ER-Golgi transport and early endoso
7 COPI mediates retrograde trafficking from the Golgi to t
8 COPI proteins oligomerize to form coated vesicles that t
9 COPI subunits immunoprecipitated with KA2 subunits from
10 COPI vesicles are generated through activation of the re
11 COPI-coated vesicles form at the Golgi apparatus from tw
12 COPI-coated vesicles mediate trafficking within the Golg
13 des a subunit of coatomer protein complex 1 (COPI) involved in intracellular traffic and autophagy.
14 ve used both site-directed mutagenesis and a COPI complex precipitation assay to demonstrate that int
15 ly, followed approximately 10 min later by a COPI component (epsilon-COP) and a trans-Golgi network (
17 termediates proceeds in two stages: first, a COPI-independent event leads to the formation of an unst
18 ulum and mitochondrial inheritance and for a COPI coatomer subunit in the targeting of a type V myosi
20 the glycoprotein ERAD signal is generated, a COPI-binding motif was appended to the N terminus of the
22 , implying that Trs120p may participate in a COPI-dependent trafficking step on the early endosomal p
23 suggest that cisternal maturation involves a COPI-dependent pathway that recycles early Golgi protein
25 l requires either COPI coatomer complex or a COPI subcomplex for translocation from the endosomal lum
30 t PGI2 production by intrarenal arterial Adv-COPI administration with renal venous clamping in female
32 se (COX)-1/prostacyclin synthase (PGIS) (Adv-COPI) gene transfer in rat kidneys with ischemia-reperfu
33 ciation of GBF1 with this compartment allows COPI recruitment and leads to its maturation into transp
36 oid legs radiating from a common center, and COPI shares with COPII highly similar vertex interaction
43 V5-tagged TMEM199 localized with ERGIC and COPI markers in HeLa cells, and electron microscopy of a
44 G complex physically interacts with GS28 and COPI and specifically binds to isolated CCD vesicles.
46 of Golgi membranes with mitotic kinases and COPI coat proteins efficiently disassembles the membrane
47 tether that connects cis-Golgi membranes and COPI-coated, retrogradely targeted intra-Golgi vesicles.
51 Our findings uncover a function for Arf1/COPI proteins at LDs and suggest a model in which Arf1/C
56 ins at LDs and suggest a model in which Arf1/COPI machinery acts to control ER-LD connections for loc
57 stituted vesicles is at least as abundant as COPI and that GAP binds directly to the dilysine motif o
60 se that neurons utilize the Golgi-associated COPI vesicle to deliver cargoes necessary for motor neur
64 he molecular nature of the interface between COPI and the nuclear pore has not been fully elucidated.
65 efinitively explore the relationship between COPI and CFTR in epithelial cells, we depleted beta-COP
66 ransport is achieved, and that bidirectional COPI transport is modulated by environmental cues throug
69 transmembrane helix 1 are essential for both COPI complex binding and the delivery of the catalytic d
71 al in cells expressing the N121I mutant, but COPI is compromised, as shown by the release of beta-COP
73 ifferent from transport vesicle formation by COPI, likely responsible for the diverse lipid droplet p
75 ediate in design between COPII and clathrin: COPI shares with clathrin an arrangement of three curved
76 ponents, including the Class I vesicle coat (COPI), the spliceosome, the proteasome, the nuclear pore
78 nt interaction between DRD3 and the coatomer COPI, a complex involved in membrane transport, and shif
82 into the ER, and the coat protein complexes (COPI and COPII), which mediate vesicular transport of pr
84 as trafficking that circumvents conventional COPI-, COPII-, and microtubule-dependent vesicular trans
85 ae with IAP (inhibitor of apoptosis) or COP (COPI coatomer, beta subunit) dsRNA silenced their target
86 ine the RNA-binding profile of Golgi-derived COPI in neuronal cells, we performed formaldehyde-linked
89 , Nup153, plays a critical role in directing COPI to the nuclear membrane at mitosis and that this ev
90 retrograde protein trafficking, we disrupted COPI functions in the Yellow Fever mosquito Aedes aegypt
92 , co-occurring KRAS and LKB1 mutation-driven COPI addiction, and selective sensitivity to a synthetic
93 elivery of LF to the cytosol requires either COPI coatomer complex or a COPI subcomplex for transloca
95 at the mu-homology domain is dispensable for COPI function in the early secretory pathway, whereas th
97 ual zinc finger is the minimal interface for COPI association, although tandem zinc fingers are optim
99 gs not only identify a new factor needed for COPI vesicle formation from Golgi membrane but also reve
102 ivity of Arf, they govern vesicle formation, COPI trafficking and the maintenance of the Golgi comple
104 ed 3D structure of a synthetically generated COPI vesicle coat obtained using cryoelectron tomography
105 ides its well-established role in generating COPI vesicles, we find that ARF1 is also involved in the
106 Furthermore, TC10 directly bound to Golgi COPI coat proteins through a dilysine motif in the carbo
108 daptor complexes and coat protein complex I (COPI) and COPII self-assemble to deform the membrane and
111 ce resembles classic coat protein complex I (COPI) coatomer protein-binding KKXX signals, and indeed
114 dibasic motif bound the coatomer complex I (COPI) in an in vitro binding assay, suggesting that ER r
116 ligand-sensitive coatomer protein complex I (COPI) retrograde trafficking complex in vitro Extensive
117 RNA helicase DDX24, and coatomer complex I (COPI) subunit ARCN1 most significantly inhibited growth
118 the gamma subunit of coat protein complex I (COPI) that is responsible for Golgi-to-ER retrograde car
120 we identify the coatomer protein complex I (COPI) vesicle coat as a critical mechanism for retention
122 llular transport via coat protein complex I (COPI), we show that COPA variants impair binding to prot
123 hat knockdown of the coat protein complex I (COPI)-Arf79F (also known as Arf1) complex selectively ki
125 We have shown that coat protein complex I (COPI)-dependent trafficking, an early step in Golgi-to-e
126 e relevance to AD of coat protein complex I (COPI)-dependent trafficking, an early step in Golgi-to-e
127 Traffic of Kv4.2 was coat protein complex I (COPI)-dependent, but KChIP1-containing vesicles were not
128 e-directed cargo but contain coat protein I (COPI) and the recycling protein p53/p58, suggesting that
129 for vesicle formation by the coat protein I (COPI) complex - a finding that reveals an unanticipated
132 efect in the localization of coat protein I (COPI) subunits, implying that Trs120p may participate in
135 and COPb proteins of the coatomer protein I (COPI) vesicle complex were reported to interact with spe
136 recent data showing that coatomer protein I (COPI) vesicle transport is involved in cellular processe
139 decreased interaction of coatomer protein I (COPI) with the hKOPR and abolished 14-3-3zeta-mediated r
141 for the interaction with coatomer protein I (COPI), which was inversely correlated with the 14-3-3 bi
142 of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the e
143 omposition of Golgi-derived coat protomer I (COPI)-coated vesicles after activating or inhibiting sig
144 d vesicles, while the COat Protein I and II (COPI and COPII) routes stand for the bidirectional traff
145 t cycles between the ER and Golgi complex in COPI and COPII vesicles, is mislocalized to the vacuole
146 ear pore basket, was found to be involved in COPI recruitment, but the molecular nature of the interf
148 ations of SEC36 are lethal with mutations in COPI subunits, indicating a functional connection betwee
151 uctures of membrane protein coats, including COPI, have been extensively studied with in vitro recons
152 ota/lambda and soluble components, including COPI (coatomer and ADP-ribosylation factor), results in
155 omotes expression of the hKOPR by inhibiting COPI and RVR motif-mediated endoplasmic reticulum locali
158 t with GOLPH3, was neither incorporated into COPI vesicles nor was dependent on GOLPH3 for proper loc
165 s early Golgi proteins, followed by multiple COPI-independent pathways that recycle late Golgi protei
175 rdinates sequential tethering and docking of COPI vesicles by first using long tethers (Golgins) and
182 Our findings demonstrate the importance of COPI-mediated transport in human development, including
185 g brefeldin A (BFA), a chemical inhibitor of COPI function, we demonstrate that short-term (1-h) BFA
186 of proteins that influence the lifecycle of COPI-coated vesicles; this conclusion is supported by th
189 bition of early endosome function by loss of COPI subunits (beta', beta, or alpha) results in accumul
192 be reversed by expressing known mediators of COPI recruitment, the GTPase ARF1 and its guanine nucleo
193 imary sequence analysis, supports a model of COPI function with significant structural and mechanisti
194 ylation factor (ARF) mediated recruitment of COPI to membranes plays a central role in transport betw
195 ARF activation to facilitate recruitment of COPI to membranes, whereas GBF1 localized at the TGN med
197 er, these demonstrate the functional role of COPI association with the SMN protein in neuronal develo
201 grade and retrograde cargoes are the size of COPI vesicles, contain coatomer, and functionally requir
203 Goldberg present X-ray crystal structures of COPI suggesting that these coats combine selected featur
205 s similar to a region in the beta-subunit of COPI coatomer complexes, which suggests the existence of
207 ts and alpha, beta', and epsilon subunits of COPI, and trace the origins of the IFT-A, IFT-B, and the
211 produced evidence for two distinct types of COPI vesicles, but the in vivo sites of operation of the
214 a suggest that the heterodimer is exposed on COPI vesicles, while the remaining part of the B-subcomp
217 ined using dsRNA directed against five other COPI coatomer subunits (alpha, beta, beta', delta, and z
220 hat is independent of its role in recruiting COPI for retrograde transport, at least of a subset of G
222 hat selectively abrogate SMN binding, retain COPI-mediated Golgi-ER trafficking functionality, but we
225 chemical studies suggested that the tapa-sin-COPI interaction regulates the retrograde transport of i
226 oci in several protein complexes (e.g., SPT, COPI, and ribosome) was posttranscriptionally controlled
229 tants yielded the surprising conclusion that COPI was dispensable both for the secretion of certain p
233 ion of the vesicular transport model is that COPI vesicles are responsible for trafficking anterograd
235 Video fluorescence microscopy revealed that COPI inactivation causes an early Golgi protein to remai
238 led to biochemical experiments, we show that COPI subunit delta (delta-COP) affects the biology of AP
239 Taken together, our findings suggest that COPI complexes likely function indirectly in influenza v
248 he Golgi apparatus is likely mediated by the COPI vesicle coat complex, but the mechanism is poorly u
249 and ubiquitously expressed gene encoding the COPI-associated protein pseudokinase SCYL1, causes an ea
250 g Xenopus extracts, we report a role for the COPI coatomer complex in nuclear envelope breakdown, imp
253 veraging, we determined the structure of the COPI coat assembled on membranes in vitro at 9 A resolut
254 yeast orthologue of the gamma subunit of the COPI coat complex (Sec21p), a known Arf1p effector.
256 ing to determine the native structure of the COPI coat within vitrified Chlamydomonas reinhardtii cel
258 P, which is best known as a component of the COPI coatamer complexes that are required for the retrog
260 arboxyl terminus of the gamma subunit of the COPI complex (gammaCOP) and describe the X-ray crystal s
263 it delta-COP function, the moderation of the COPI-dependent trafficking in vivo leads to a significan
264 Secretory protein trafficking relies on the COPI coat, which by assembling into a lattice on Golgi m
267 Golgi-to-ER recycling of WLS requires the COPI regulator ARF as well as ERGIC2, an ER-Golgi interm
270 al and molecular experiments showed that the COPI retrograde complex regulates ligand-mediated AR tra
272 e show that WDR35 has strong homology to the COPI coatamers involved in vesicular trafficking and tha
273 e lysine-rich transmembrane helix 1 with the COPI binding portion of the p23 adaptor cytoplasmic tail
274 does not influence its interaction with the COPI coat or efficient recruitment onto transport vesicl
276 the same entry defects as observed with the COPI-depleted cells but did result in specific decreases
279 ability of transmembrane helix 1 to bind to COPI complex appears to be the essential feature for cat
280 ound to coatomer, inhibits dynein binding to COPI vesicles whereas preventing the coatomer-Cdc42 inte
281 r domain from an unrelated protein, binds to COPI and dominantly inhibits progression of nuclear enve
282 nonredundant roles, perhaps contributing to COPI recruitment platforms on both the nuclear and cytop
283 o a region within Nup153 that is critical to COPI association, yet inspection of these two zinc finge
285 duction, we found that prolonged exposure to COPI complex disruption through siRNA depletion resulted
286 regions of the protein, we localized GIV to COPI, endoplasmic reticulum (ER)-Golgi transport vesicle
288 hinery components are returned to the ER via COPI-coated vesicles, which undergo similar tethering an
292 Our results offer an explanation of why COPI coatomer is frequently identified in screens for ce
293 l Galpha-interacting protein associated with COPI transport vesicles that may play a role in Galpha-m
295 ripheral Golgi protein able to interact with COPI coat as well as with a binding motif present in the
299 ticulum and the Golgi involves vesicles with COPI and COPII coats, whereas clathrin is the predominan
300 Previous studies of thermosensitive yeast COPI mutants yielded the surprising conclusion that COPI
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