期刊
SCIENCE
卷 340, 期 6130, 页码 356-359出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1234264
关键词
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资金
- Wellcome Trust
- London Law Trust
- British Heart Foundation
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.
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