Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies.

@article{Pankiv2010NucleocytoplasmicSO,
  title={Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies.},
  author={Serhiy Pankiv and Trond Lamark and Jack-Ansgar Bruun and Aud \Overvatn and Geir Bj\ork\oy and Terje Johansen},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 8},
  pages={5941-53}
}
p62, also known as sequestosome1 (SQSTM1), A170, or ZIP, is a multifunctional protein implicated in several signal transduction pathways. p62 is induced by various forms of cellular stress, is degraded by autophagy, and acts as a cargo receptor for autophagic degradation of ubiquitinated targets. It is also suggested to shuttle ubiquitinated proteins for proteasomal degradation. p62 is commonly found in cytosolic protein inclusions in patients with protein aggregopathies, it is up-regulated in… CONTINUE READING

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