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Single-handed recognition of a sorting traffic motif by the GGA proteins

Nature Structural Biology volume 9, pages 241–244 (2002)Cite this article

Selective transport of cargo between membrane-bound organelles is vital for the well-being of cells. The crystal structure of a short peptide signal from the cytoplasmic tail of the mannose-6-phosphate receptor bound to the VHS domain of GGA proteins gives hints to how sorting works.

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Figure 1: The major routes that use vesicles and tubulo-vesicular carriers to traffic cargo molecules along the biosynthetic and endocytic pathways.
Figure 2: GGAs as adaptors that link coat formation with cargo sorting.

Bob Crimi

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  1. the Department of Cell Biology, Harvard Medical School and The Center for Blood Research, Boston, 02115, Massachusetts, USA

    Tom Kirchhausen

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Kirchhausen, T. Single-handed recognition of a sorting traffic motif by the GGA proteins. Nat Struct Mol Biol 9, 241–244 (2002). https://doi.org/10.1038/nsb0402-241

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