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Biology of the Endoplasmic Reticulum

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Book cover Endoplasmic Reticulum Stress in Health and Disease

Abstract

Since its discovery in 1945, our knowledge of the structure and many functions of the endoplasmic reticulum (ER) has advanced at a phenomenal rate. Early studies focused on the structure, which was then followed by biochemical and functional studies associated with calcium storage and release from the ER, protein folding and secretion, ER associated degradation (ERAD) and ER stress responses. Currently there is a significant interest in the role of ER in such cellular processes as cell death, autophagy and cross-talk with other organelles. In this chapter we give an overview of the structural characteristics and biochemical functioning of the ER and describe its manifold roles in cellular physiology. Finally, we explain how the sensitive nature of the protein folding process in the ER enables this organelle to act as a sensor of a broad range of cellular stresses. Signals emanating from the stressed ER play central roles in differentiation processes, cellular homeostasis and cell death.

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Abbreviations

ATF:

Activating transcription factor

CNX:

Calnexin

COPII:

Coat protein II

CRT:

Calreticulin

CYP:

Cytochrome p-450

ER:

Endoplasmic reticulum

ERAD:

ER associated degradation

ERAF:

ER associated folding

GRP:

Glucose regulated protein

GSH:

Glutathione

HSP:

Heat shock protein

IP3R:

Inositol trisphosphate receptor

IRE1:

Inositol-requiring enzyme 1

PDI:

Protein disulfide isomerase

PERK:

Pancreatic ER kinase-like ER kinase

PM:

Plasma membrane

PPIs:

Peptidyl-prolyl cis-trans isomerase

RER:

Rough ER

RYR:

Ryanodine receptor

SER:

Smooth ER

SERCA:

Sarco-endoplasmic reticulum activated Ca2+pump

SNARE:

Soluble N-ethylmaleimide-sensitive factor attachment protein receptor

SR:

Sarcoplasmic reticulum

SREBPs:

Sterol regulatory element binding proteins

TAC:

Tip attachment complex

tER:

Transitional ER

UGGT:

UDP-Glc:glycoprotein glucosyltransferase

UGT:

UDP-glucuronyl transferase

UPR:

Unfolded protein response

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Authors and Affiliations

  1. Apoptosis Research Center, National University of Ireland, Galway, Ireland

    Sandra JM Healy, Richard Jäger & Afshin Samali

  2. Cell Death Research & Therapy Unit, Department of Cellular and Molecular Medicine, Catholic University of Leuven, Leuven, Belgium

    Tom Verfaillie & Patrizia Agostinis

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  2. Tom Verfaillie
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  3. Richard Jäger
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  4. Patrizia Agostinis
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  5. Afshin Samali
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Corresponding author

Correspondence to Patrizia Agostinis .

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Editors and Affiliations

  1. Dept Molec Cell Bio, K.U. Leuven, Harestraat/Gasthuisberg, B-3000 Leuven, 3000, Belgium

    Patrizia Agostinis

  2. School of Natural Science, Department of Biochemistry, NUI Galway, University Road, Galway, Ireland

    Samali Afshin

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© 2012 Springer Science+Business Media Dordrecht

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Healy, S.J., Verfaillie, T., Jäger, R., Agostinis, P., Samali, A. (2012). Biology of the Endoplasmic Reticulum. In: Agostinis, P., Afshin, S. (eds) Endoplasmic Reticulum Stress in Health and Disease. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4351-9_1

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