Arf1-GTP-induced Tubule Formation Suggests a Function of Arf Family Proteins in Curvature Acquisition at Sites of Vesicle Budding
ADP-ribosylation factor (Arf) and related small GTPases play crucial roles in membrane traffic within the exo- and endocytic pathways. Arf proteins in their GTP-bound state are associated with curved membrane buds and tubules, frequently together with effector coat proteins to which they bind. Here...
Saved in:
Published in: | The Journal of biological chemistry Vol. 283; no. 41; pp. 27717 - 27723 |
---|---|
Main Authors: | , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Elsevier Inc
10-10-2008
American Society for Biochemistry and Molecular Biology |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | ADP-ribosylation factor (Arf) and related small GTPases play crucial roles in membrane traffic within the exo- and endocytic pathways. Arf proteins in their GTP-bound state are associated with curved membrane buds and tubules, frequently together with effector coat proteins to which they bind. Here we report that Arf1 is found on membrane tubules originating from the Golgi complex where it colocalizes with COPI and GGA1 vesicle coat proteins. Arf1 also induces tubulation of liposomes in vitro. Mutations within the amino-terminal amphipathic helix (NTH) of Arf1 affect the number of Arf1-positive tubules in vivo and its property to tubulate liposomes. Moreover, hydrophilic substitutions within the hydrophobic part of its NTH impair Arf1-catalyzed budding of COPI vesicles in vitro. Our data indicate that GTP-controlled local induction of high curvature membranes is an important property of Arf1 that might be shared by a subgroup of Arf/Arl family GTPases. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this study. Recipient of a long term fellowship from EMBO and a Human Frontier Science Program Organization (HFSPO) cross-disciplinary postdoctoral fellowship. Present address: Physico-Chemistry Dept., UMR 168, CNRS/Institut Curie, 75005 Paris, France. |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.M804528200 |