2JX0

The paxillin-binding domain (PBD) of G Protein Coupled Receptor (GPCR)-kinase (GRK) interacting protein 1 (GIT1)

2JX0 の概要

• エントリーDOI: 10.2210/pdb2jx0/pdb
• 分子名称: ARF GTPase-activating protein GIT1 (1 entity in total)
• 機能のキーワード: paxillin binding domain homologue, ank repeat, cytoplasm, gtpase activation, metal-binding, phosphorylation, zinc, zinc-finger, cell adhesion, signaling protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm (By similarity): Q9Z272
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15029.24

構造登録者

Zhang, Z.,Guibao, C.D.,Simmerman, J.A.,Zheng, J. (登録日: 2007-11-01, 公開日: 2008-04-29, 最終更新日: 2024-05-29)

主引用文献

Zhang, Z.M.,Simmerman, J.A.,Guibao, C.D.,Zheng, J.J.
GIT1 paxillin-binding domain is a four-helix bundle, and it binds to both paxillin LD2 and LD4 motifs.
J.Biol.Chem., 283:18685-18693, 2008

PubMed Abstract: The G protein-coupled receptor kinase-interacting protein 1 (GIT1) is a multidomain protein that plays an important role in cell adhesion, motility, cytoskeletal remodeling, and membrane trafficking. GIT1 mediates the localization of the p21-activated kinase (PAK) and PAK-interactive exchange factor to focal adhesions, and its activation is regulated by the interaction between its C-terminal paxillin-binding domain (PBD) and the LD motifs of paxillin. In this study, we determined the solution structure of rat GIT1 PBD by NMR spectroscopy. The PBD folds into a four-helix bundle, which is structurally similar to the focal adhesion targeting and vinculin tail domains. Previous studies showed that GIT1 interacts with paxillin through the LD4 motif. Here, we demonstrated that in addition to the LD4 motif, the GIT1 PBD can also bind to the paxillin LD2 motif, and both LD2 and LD4 motifs competitively target the same site on the PBD surface. We also revealed that paxillin Ser(272) phosphorylation does not influence GIT1 PBD binding in vitro. These results are in agreement with the notion that phosphorylation of paxillin Ser(272) plays an essential role in regulating focal adhesion turnover.

PubMed: 18448431
DOI: 10.1074/jbc.M801274200

実験手法

SOLUTION NMR