Structural basis for kinesin-1:cargo recognition

Stefano Pernigo, Anneri Lamprecht, Roberto A Steiner, Mark P Dodding

Research output: Contribution to journalArticle (Academic Journal)peer-review

45 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)356-9
Number of pages4
JournalScience
Volume340
Issue number6130
DOIs
Publication statusPublished - 19 Apr 2013

Keywords

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins
  • Crystallography, X-Ray
  • Glycoproteins
  • HeLa Cells
  • Humans
  • Mice
  • Microtubule-Associated Proteins
  • Molecular Sequence Data
  • Mutation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Tryptophan
  • Journal Article
  • Research Support, Non-U.S. Gov't

Fingerprint Dive into the research topics of 'Structural basis for kinesin-1:cargo recognition'. Together they form a unique fingerprint.

Cite this