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PubMed:11950392 JSONTXT 2 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-120 Sentence denotes GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.
T2 121-251 Sentence denotes ADP-ribosylation factors (ARFs) are a family of small GTPases that are involved in various aspects of membrane trafficking events.
T3 252-366 Sentence denotes These include ARF1-ARF6, which are divided into three classes on the basis of similarity in the primary structure:
T4 367-432 Sentence denotes Class I, ARF1-ARF3; Class II, ARF4 and ARF5; and Class III, ARF6.
T5 433-762 Sentence denotes Previous studies identified a novel family of potential ARF effectors, termed GGA1-GGA3, which interact specifically with GTP-bound ARF1 and ARF3 and are localized to the trans-Golgi network (TGN) or its related compartment(s) (GGA is an abbreviation for Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding protein).
T6 763-954 Sentence denotes In the present study we have shown that ARF proteins belonging to the three classes, ARF1, ARF5 and ARF6, can interact with all GGA proteins in a yeast two-hybrid assay, in vitro and in vivo.
T7 955-1173 Sentence denotes Segmentation of GGA proteins and isolation of GGA mutants defective in ARF binding have revealed that a limited region within the GGA homology domain, which is conserved in the GGA family, is essential for ARF binding.
T8 1174-1314 Sentence denotes Expression in cells of GTPase-restricted mutants of ARF1 and ARF5 blocks dissociation of GGA proteins from membranes induced by brefeldin A.
T9 1315-1397 Sentence denotes However, neither of the ARF mutants recruits GGA mutants defective in ARF binding.
T10 1398-1574 Sentence denotes On the basis of these observations, we conclude that at least ARF1 (Class I) and ARF5 (Class II) in their GTP-bound state cause recruitment of GGA proteins on to TGN membranes.
T11 1575-1737 Sentence denotes In contrast, on the basis of similar experiments, ARF6 (Class III) may be involved in recruitment of GGA proteins to other compartments, possibly early endosomes.