• DOI:10.1016/S0960-9822(02)00764-9
Corpus ID: 9977605

A Conserved Interaction between β1 Integrin/PAT-3 and Nck-Interacting Kinase/MIG-15 that Mediates Commissural Axon Navigation in C. elegans

@article{Poinat2002ACI,
  title={A Conserved Interaction between β1 Integrin/PAT-3 and Nck-Interacting Kinase/MIG-15 that Mediates Commissural Axon Navigation in C. elegans},
  author={Patrice Poinat and A. Arcangelis and S. Sookhareea and X. Zhu and E. Hedgecock and M. Labouesse and E. Georges-Labouesse},
  journal={Current Biology},
  year={2002},
  volume={12},
  pages={622-631}
}

Patrice Poinat, A. Arcangelis, +4 authors E. Georges-Labouesse

Published 2002

Biology, Medicine

Current Biology

BACKGROUND Integrins are heterodimeric (alphabeta) transmembrane receptors for extracellular matrix (ECM) ligands. Through interactions with molecular partners at cell junctions, they provide a connection between the ECM and the cytoskeleton and regulate many aspects of cell behavior. A number of integrin-associated molecules have been identified; however, in many cases, their function and role in the animal remain to be clarified. RESULTS We have identified the Nck-interacting kinase (NIK… CONTINUE READING

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