| First Author | Pernigo S | Year | 2013 |
| Journal | Science | Volume | 340 |
| Issue | 6130 | Pages | 356-9 |
| PubMed ID | 23519214 | Mgi Jnum | J:245359 |
| Mgi Id | MGI:5918671 | Doi | 10.1126/science.1234264 |
| Citation | Pernigo S, et al. (2013) Structural basis for kinesin-1:cargo recognition. Science 340(6130):356-9 |
| abstractText | 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. |
