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Publication - Dr Mark Dodding

    Structural basis for kinesin-1:cargo recognition

    Citation

    Pernigo, S, Lamprecht, A, Steiner, RA & Dodding, MP, 2013, ‘Structural basis for kinesin-1:cargo recognition’. Science, vol 340., pp. 356-9

    Abstract

    Kinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat domain of kinesin light chain 2 in complex with a cargo peptide harboring a "tryptophan-acidic" motif derived from SKIP (SifA-kinesin interacting protein), a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition.

    Full details in the University publications repository