2006年10月
Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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- 巻
- 103
- 号
- 42
- 開始ページ
- 15416
- 終了ページ
- 15421
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1073/pnas.0605357103
- 出版者・発行元
- NATL ACAD SCIENCES
Family of Rabl1-interacting protein (FIP)3/Arfophlin-1 and FIP4/ Arfophilin-2 are dual effectors for Rabll and ADP ribosylation factor (ARF)5/ARF6, which are involved in membrane delivery from recycling enclosomes to the plasma membrane during cytokinesis. Here, we define the distinct C-terminal binding regions of FIP3 and FIP4 for Rabll and ARF5/ARF6. Furthermore, we determined the crystal structure of Rab11 in complex with the Rabll-binding domain (REID) of FIP3. The long amphiphilic alpha-helix of FIP3-RBD forms a parallel coiled-coil homodimer, with two symmetric interfaces with two Rabl 1 molecules. The hydrophobic side of the RBD helix is involved in homodimerization and mediates the interaction with the Rabll 1 switch 1 region, whereas the opposite hydrophilic side interacts with the Rabll switch 2 and is the major factor contributing to the binding specificity. The bivalent interaction of FlP3 with Rabll at the C terminus allows FlP3 to coordinately function with other binding partners, including ARFs.
- リンク情報
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- DOI
- https://doi.org/10.1073/pnas.0605357103
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000241476200027&DestApp=WOS_CPL
- URL
- http://www.scopus.com/inward/record.url?eid=2-s2.0-33750365184&partnerID=MN8TOARS
- URL
- http://orcid.org/0000-0001-7701-7183
- ID情報
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- DOI : 10.1073/pnas.0605357103
- ISSN : 0027-8424
- ORCIDのPut Code : 44277935
- SCOPUS ID : 33750365184
- Web of Science ID : WOS:000241476200027