Journal Article

PreJuSER-6509

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure and potential functions of GABARAP

Mohrlüder, J.FZJ* ; Schwarten, M.FZJ* ; Willbold, D.FZJ*

2009
Wiley-Blackwell Oxford [u.a.]

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Please use a persistent id in citations: doi:10.1111/j.1742-4658.2009.07207.x

Abstract: The gamma-aminobutyrate type A receptor-associated protein (GABARAP) is a ubiquitin-like modifier, and is implicated in a variety of membrane trafficking and fusion events that are crucial to synaptic plasticity, autophagy and apoptosis. However, important aspects of GABARAP function and regulation remain poorly understood. We review the current state of knowledge about GABARAP, highlighting newly-identified GABARAP ligands, and discuss the possible physiological relevance of each ligand interaction.

Keyword(s): Adaptor Proteins, Signal Transducing: chemistry (MeSH) ; Adaptor Proteins, Signal Transducing: physiology (MeSH) ; Animals (MeSH) ; Calreticulin: physiology (MeSH) ; Carrier Proteins: physiology (MeSH) ; Humans (MeSH) ; Ligands (MeSH) ; Membrane Proteins: physiology (MeSH) ; Microfilament Proteins: physiology (MeSH) ; Microtubule-Associated Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: physiology (MeSH) ; Nerve Tissue Proteins: physiology (MeSH) ; Receptors, GABA-A: physiology (MeSH) ; Adaptor Proteins, Signal Transducing ; Calreticulin ; Carrier Proteins ; GABARAP protein, human ; GABARAPL2 protein, human ; GABRG2 protein, human ; GRIP1 protein, human ; Ligands ; Membrane Proteins ; Microfilament Proteins ; Microtubule-Associated Proteins ; Nerve Tissue Proteins ; Receptors, GABA-A ; gephyrin ; J ; apoptosis (auto) ; autophagy (auto) ; GABA(A) receptor (auto) ; GABARAP (auto) ; protein structure (auto) ; protein-protein interaction (auto) ; trafficking (auto)

Note: The authors thank Sameer Singh for carefully reading the manuscript. This study was supported by a fellowship of the International Helmholtz Research School BioSoft to M. Schwarten and a research grant from the Deutsche Forschungsgemeinschaft (DFG) to D. Willbold (Wi1472/5).

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Contributing Institute(s):

1. Strukturbiochemie (ISB-3)
2. Jülich Aachen Research Alliance - High-Performance Computing (JARA-HPC)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2009

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