Home > B. Cellular pathology > Endoplasmic reticulum
Endoplasmic reticulum
Monday 9 June 2003
The endoplasmic reticulum (ER) is an extensive three-dimensional network that stretches from the inner nuclear envelope to the cell cortex with a single, continuous membrane and a single, continuous lumen. The ER contains specialized regions that carry out unique functions.
Types
smooth endoplasmic reticulum (SER)
rough endoplasmic reticulum (RER)
Pathology
endoplasmic reticulum stress
-
RNA translation diseases
- Wolcott-Rallison syndrome
endoplasmic reticulum retention
- alpha1-anti-trypsin deficiency (alpha1AT deficiency) variants exhibit a selective defect in migration of this secretory protein from the endoplasmic reticulum (ER) to Golgi apparatus.
- This is most marked for the PiZ polypeptide, attributable to a single amino acid substitution of Glu342 to Lys342. The mutant polypeptide (α1AT-Z) is abnormally folded, and polymerizes, causing its retention in the ER. All individuals with the PiZZ genotype accumulate α1AT-Z in the ER of hepatocytes.
See also
cellular organelles
reticulum endoplasmic stress
ER protein transport
References
Pizzo P, Pozzan T. Mitochondria-endoplasmic reticulum choreography: structure and signaling dynamics. Trends Cell Biol. 2007 Oct;17(10):511-7. PMID: 17851078
Zimmermann R, Muller L, Wullich B. Protein transport into the endoplasmic reticulum: mechanisms and pathologies. Trends Mol Med. 2006 Dec;12(12):567-73. PMID: 17071140
Federovitch CM, Ron D, Hampton RY. The dynamic ER: experimental approaches and current questions. Curr Opin Cell Biol. 2005 Aug;17(4):409-14. PMID: 15975777
Levine T, Rabouille C. Endoplasmic reticulum: one continuous network compartmentalized by extrinsic cues. Curr Opin Cell Biol. 2005 Aug;17(4):362-8. PMID: 15975783
Shi Y, Taylor SI, Tan SL, Sonenberg N. When translation meets metabolism: multiple links to diabetes. Endocr Rev. 2003 Feb;24(1):91-101. PMID: 12588811
Harding HP, Ron D. Endoplasmic reticulum stress and the development of diabetes: a review. Diabetes. 2002 Dec;51 Suppl 3:S455-61. PMID: 12475790
Drenth JP, Martina JA, van de Kerkhof R, Bonifacino JS, Jansen JB. Polycystic liver disease is a disorder of cotranslational protein processing. Trends Mol Med. 2005 Jan;11(1):37-42. PMID: 15649821
Hebert DN, Garman SC, Molinari M. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 2005 Jul;15(7):364-70. PMID: 15939591
Rao RV, Bredesen DE. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol. 2004 Dec;16(6):653-62. PMID: 15530777
Palmer KJ, Stephens DJ. Biogenesis of ER-to-Golgi transport carriers: complex roles of COPII in ER export. Trends Cell Biol. 2004 Feb;14(2):57-61. PMID: 15106609
Berridge MJ. The endoplasmic reticulum: a multifunctional signaling organelle. Cell Calcium. 2002 Nov-Dec;32(5-6):235-49. PMID: 12543086
Thinakaran G. Metabolism of presenilins. J Mol Neurosci. 2001 Oct;17(2):183-92. PMID: 11816791
Patil C, Walter P: Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13:349, 2001.