Journal Article

PreJuSER-5170

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural framework of the GABARAP-calreticulin interface - implications for substrate binding to endoplasmic reticulum chaperones

Thielmann, Y.FZJ* ; Weiergräber, O. H.FZJ* ; Mohrlüder, J.FZJ* ; Willbold, D.FZJ*

2009
Wiley-Blackwell Oxford [u.a.]

This record in other databases:      

Please use a persistent id in citations: doi:10.1111/j.1742-4658.2008.06857.x

Abstract: The 4-aminobutyrate type A receptor-associated protein (GABARAP) is a versatile adaptor protein that plays an important role in intracellular vesicle trafficking, particularly in neuronal cells. We have investigated the structural determinants underlying the interaction of GABARAP with calreticulin using spectroscopic and crystallographic techniques. Specifically, we present the crystal structure of GABARAP in complex with its major binding epitope on the chaperone. Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general.

Keyword(s): Adaptor Proteins, Signal Transducing: chemistry (MeSH) ; Adaptor Proteins, Signal Transducing: metabolism (MeSH) ; Calreticulin: chemistry (MeSH) ; Calreticulin: metabolism (MeSH) ; Endoplasmic Reticulum: metabolism (MeSH) ; Humans (MeSH) ; Microtubule-Associated Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: metabolism (MeSH) ; Models, Molecular (MeSH) ; Molecular Chaperones: chemistry (MeSH) ; Molecular Chaperones: metabolism (MeSH) ; Protein Binding (MeSH) ; Substrate Specificity (MeSH) ; Adaptor Proteins, Signal Transducing ; Calreticulin ; GABARAP protein, human ; Microtubule-Associated Proteins ; Molecular Chaperones ; J ; 4-aminobutyrate type A receptor-associated protein (GABARAP) (auto) ; calreticulin (auto) ; protein-protein interaction (auto) ; structure model (auto) ; X-ray crystallography (auto)

Note: The authors wish to thank Olga Dietz for excellent technical assistance. O. H. WeiergrAber is grateful to Georg Buldt for continuous generous support. Moreover, assistance by the ESRF staff at beamline ID14-1 is acknowledged. This study was supported by a research grant from the Deutsche Forschungsgemeinschaft (DFG) to D. Willbold (Wi1472/5).

---

Contributing Institute(s):

1. Molekulare Biophysik (ISB-2)
2. Jülich Aachen Research Alliance - High-Performance Computing (JARA-HPC)

Research Program(s):

1. Programm Biosoft (N03)

Appears in the scientific report 2009
Notes: übergangsweise lautet die FE-Bezeichnung für das ISB-2 N03

---