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Structure‐function investigation of PI(4)P binding proteins
Author(s) -
Scott Jordan Leslie,
He Ju,
Kutateladze Tatiana,
Stahelin Robert
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.939.6
Subject(s) - golgi apparatus , signal transducing adaptor protein , clathrin , golgi membrane , copi , clathrin adaptor proteins , pi , chemistry , biophysics , vesicle , plasma protein binding , microbiology and biotechnology , biochemistry , membrane , biology , receptor , secretory pathway , endoplasmic reticulum
ADP‐ribosylation factor 1 (Arf1) and four phosphate adaptor protein (FAPP1) are known to co‐localize at the trans‐golgi network and be involved in the process of membrane traffic from the golgi to the plasma membrane. Arf1is a 21 kDa protein known to act in the recruitment of coat proteins and the coating of cargo vesicles by interacting with coatomer and clathrin‐adaptor complex proteins. FAPP1, a 34 kDa protein harboring a phosphotidyl‐4‐phosphate (PI4P) binding PH domain has recently been shown to alter membrane shape in a PI4P‐dependent manner. Though crystal structures are available for both individual proteins, their structural and biophysical interaction has not been elucidated. In collaboration with the Kutateladze lab we have investigated the structural interaction between FAPP1 and Arf1 using X‐ray, NMR, and biophysical analysis. Results demonstrate a high affinity interaction between the active form of Arf 1 and the PH domain of FAPP1. The specificity of the Arf1‐FAPP1 interaction as well as an expansion of PI(4)P‐binding proteins in general will be presented.