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Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5

✍ Scribed by Zhu, Guangyu (author);Chen, Jia (author);Liu, Jay (author);Brunzelle, Joseph S. (author);Huang, Bo (author);Wakeham, Nancy (author);Terzyan, Simon (author);Li, Xuemei (author);Rao, Zihe (author);Li, Guangpu (author);Zhang, Xuejun C. (author)

Book ID
110032143
Publisher
Nature Publishing Group
Year
2007
Tongue
English
Weight
433 KB
Volume
26
Category
Article
ISSN
0261-4189

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Structure of the APPL1 BAR-PH domain and
Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5
✍ Zhu, Guangyu (author);Chen, Jia (author);Liu, Jay (author);Brunzelle, Joseph S. πŸ“‚ Article πŸ“… 2007 πŸ› Nature Publishing Group 🌐 English βš– 433 KB

APPL1 is an effector of the small GTPase Rab5. Together, they mediate a signal transduction pathway initiated by ligand binding to cell surface receptors. Interaction with Rab5 is confined to the amino (N)-terminal region of APPL1. We report the crystal structures of human APPL1 N-terminal BAR-PH do