| 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. |