Journal Article

FZJ-2015-06975

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy

Schwarten, M.FZJ* ; Mohrlüder, J.FZJ* ; Ma, P. ; Stoldt, M.FZJ* ; Thielmann, Y. ; Stangler, T. ; Hersch, N.FZJ* ; Hoffmann, B.FZJ* ; Merkel, R.FZJ* ; Willbold, D. (Corresponding author)FZJ*

2009
Taylor & Francis Abingdon, Oxon

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Please use a persistent id in citations: doi:10.4161/auto.5.5.8494

Abstract: Autophagy, a pathway primarily relevant for cell survival, and apoptosis, a process invariably leading to cell death, are the two main mechanisms of cellular self-destruction, which are essential in cell growth, neurodegeneration, tumor suppression, stress and immune response. Currently, a potential crosstalk between apoptosis and autophagy is subject to intensive investigations since recently some direct junctions became obvious. The respective protein-protein interaction network, however, remains to be elucidated in detail. The γ-aminobutyric acid type A (GABAA) receptor-associated protein GABARAP belongs to a family of proteins implicated in intracellular transport events and was shown to be associated to autophagic processes. Using a phage display screening against the target protein GABARAP, we identified the proapoptotic protein Nix/Bnip3L to be a potential GABARAP ligand. In vitro binding studies, pull-down analysis,coimmunoprecipitation assays and colocalization studies confirmed a direct interaction of both proteins in mammalian cells.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)
2. Biomechanik (ICS-7)

Research Program(s):

1. 552 - Engineering Cell Function (POF3-552) (POF3-552)

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Database coverage:
; BIOSIS Previews ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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