LC8 dynein light chain (DYNLL1) binds to the C-terminal domain of ATM-interacting protein (ATMIN/ASCIZ) and regulates its subcellular localization.

@article{Rapali2011LC8DL,
  title={LC8 dynein light chain (DYNLL1) binds to the C-terminal domain of ATM-interacting protein (ATMIN/ASCIZ) and regulates its subcellular localization.},
  author={P{\'e}ter Rapali and M{\^a}ria Flor Garc{\'i}a-Mayoral and M{\'o}nica Mart{\'i}nez-Moreno and Kriszti{\'a}n T{\'a}rnok and Katalin Schlett and Juan P. Albar and Marta Bruix and L{\'a}szl{\'o} Nyitray and Ignacio Rodr{\'i}guez-Crespo},
  journal={Biochemical and biophysical research communications},
  year={2011},
  volume={414 3},
  pages={493-8}
}
LC8 dynein light chain (now termed DYNLL1 and DYNLL2 in mammals), a dimeric 89 amino acid protein, is a component of the dynein multi-protein complex. However a substantial amount of DYNLL1 is not associated to microtubules and it can thus interact with dozens of cellular and viral proteins that display well-defined, short linear motifs. Using DYNLL1 as bait in a yeast two-hybrid screen of a human heart library we identified ATMIN, an ATM kinase-interacting protein, as a DYNLL1-binding partner… CONTINUE READING
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