Site-Specific Cross-Linking Reveals a Differential Direct Interaction of Class 1, 2, and 3 ADP-Ribosylation Factors with Adaptor Protein Complexes 1 and 3
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- 作者：Carol Austin ; Markus Boehm ; and Sharon A. Tooze
- 刊名：Biochemistry
- 出版年：2002
- 出版时间：April 9, 2002
- 年：2002
- 卷：41
- 期：14
- 页码：4669 - 4677
- 全文大小：233K
- 年卷期：v.41,no.14(April 9, 2002)
- ISSN：1520-4995
文摘
We have used a site-specific photo-cross-linking approach to identify direct interactions betweenclathrin adaptor protein (AP)1 complexes and small GTPases of the ADP-ribosylation factor (ARF) familyand to explore the specificity of this interaction on immature secretory granule (ISG) membranes. ISGmembranes are a well-characterized, highly enriched preparation of membranes that has previously beenshown to have the membrane-associated factors for ARF1 recruitment that are not present on artificialliposomes. All three classes of ARF proteins could be recruited to ISG membranes, displaying differentialrequirements for GTP
S. We found that ARF1, ARF5, and ARF6 interacted directly with the 
1-adaptinsubunit of AP-1 in the presence of GTPS. Furthermore, we observed a direct interaction between theswitch 1 region of ARF1 and the N-terminal trunk domains of - and 1-adaptin. In addition, both ARF1and ARF6 but not ARF5 interacted directly with the 3- and 
-adaptin subunits of AP-3. No interactionwas observed between AP-2 and any of the ARF proteins. Our results delineate the specificity and provideevidence of a direct interaction between different ARF proteins and the AP complexes AP-1 and AP-3 onnatural ISG membranes and show that residues in the switch 1 region of ARF proteins can selectivelybind to the trunk domains of these complexes.
S. We found that ARF1, ARF5, and ARF6 interacted directly with the 1-adaptinsubunit of AP-1 in the presence of GTPS. Furthermore, we observed a direct interaction between theswitch 1 region of ARF1 and the N-terminal trunk domains of - and 1-adaptin. In addition, both ARF1and ARF6 but not ARF5 interacted directly with the 3- and -adaptin subunits of AP-3. No interactionwas observed between AP-2 and any of the ARF proteins. Our results delineate the specificity and provideevidence of a direct interaction between different ARF proteins and the AP complexes AP-1 and AP-3 onnatural ISG membranes and show that residues in the switch 1 region of ARF proteins can selectivelybind to the trunk domains of these complexes.