Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Unfolded Protein Response and Cancer

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_6108-2

Definition

Endoplasmic reticulum (ER) is an organelle consisting of membranous networks that connect to the outer nuclear envelop of the nucleus and is found throughout the cell. These interconnected membranes form sacs or tubes known as cisternae. ER is present in eukaryotic cells except for the red blood cells and spermatozoa (sperm cells), but not in the prokaryotic cells.

The ER is essential for the storage and regulated release of intracellular calcium. ER is also the main subcellular compartment where newly synthesized proteins undergo proper folding and maturation prior to exit from ER and transport to the Golgi apparatus or the cellular membrane. Normally, only the properly folded proteins are transported from the ER. Correct folding of newly synthesized is carried out by several endoplasmic reticulum chaperone proteins, including protein disulfide isomerase (PDI), ERp29, the HSP70 family member BIP/GRP78, calnexin, calreticulin, and the peptidylpropyl isomerase family....

Keywords

Unfold Protein Response Endoplasmic Reticulum Chaperone Unfold Protein Response Activation Unfold Protein Response Pathway Perk Activation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Hetz C, Chevet E, Harding HP (2013) Targeting the unfolded protein response in disease. Nat Rev Drug Discov 12(9):703–719CrossRefPubMedGoogle Scholar
  2. Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J (1998) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332(6163):462–464CrossRefGoogle Scholar
  3. Vandewynckel YP, Laukens D, Geerts A, Bogaerts E, Paridaens A, Verhelst X, Janssens S, Heindryckx F, Van Vlierberghe H (2013) The paradox of the unfolded protein response in cancer. Anticancer Res 33(11):4683–4694PubMedGoogle Scholar
  4. Walter P, Ron D (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334(6059):1081–1086CrossRefPubMedGoogle Scholar
  5. Wang M, Kaufman RJ (2014) The impact of the endoplasmic reticulum protein-folding environment on cancer development. Nat Rev Cancer 14(9):581–597CrossRefPubMedGoogle Scholar

See Also

  1. (2012) Endoplasmic reticulum stress response. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1244. doi:10.1007/978-3-642-16483-5_1889Google Scholar
  2. (2012) ER-associated protein degradation. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1307. doi:10.1007/978-3-642-16483-5_1981Google Scholar
  3. (2012) PERK. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, pp 2819–2820. doi:10.1007/978-3-642-16483-5_4469Google Scholar
  4. (2012) IRE1. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 1912. doi:10.1007/978-3-642-16483-5_3145Google Scholar
  5. (2012) ATF6. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 299. doi:10.1007/978-3-642-16483-5_430Google Scholar
  6. (2012) BiP/GRp78. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 416. doi:10.1007/978-3-642-16483-5_652Google Scholar
  7. (2012) Unfolded protein response. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 3846. doi:10.1007/978-3-642-16483-5_6108Google Scholar
  8. (2012) C/EBP homologous protein. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer, Berlin/Heidelberg, p 720. doi:10.1007/978-3-642-16483-5_981Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular MedicineThe George Washington UniversityWashingtonUSA