|
|
|
|
 |
|||
|
|||
Immunocytochemical localization of BiP to the rough endoplasmic reticulum: evidence for protein sorting by selective retention
DG Bole, R Dowin, M Doriaux and JD Jamieson
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510.
Immunoglobulin heavy chain binding protein (BiP) (also known as GRP 78) is a protein of the endoplasmic reticulum (ER) which has been shown to be involved in post-translational processing of nascent membrane and secretory proteins. To determine BiP's location in the exocytic pathway, we localized BiP at the electron microscopic level in mouse myeloma cell lines by immunoperoxidase cytochemistry. BiP was found to be present within the cisternal spaces of the RER and nuclear envelope but was not detected in the cisternae of the Golgi complex. BiP reaction product was also found within transitional elements of the RER but was absent from smooth-surfaced vesicles found between the ER and the Golgi complex. Immunoperoxidase staining of BiP was reduced or absent in regions of a smooth ER membrane system in myelomas that contained endogenous murine retrovirus A particles. All compartments of the exocytic pathway, including the virus-containing smooth ER, stained for IgG, a secretory protein. These observations suggest that BiP is selectively retained in the cisternae of the ER and is not free to enter Golgi-directed transport vesicles. These studies suggest that BiP's subcellular localization may occur by selective interaction with component(s) of the ER.
Volume 37,
Issue 12,
pp. 1817-1823,
12/01/1989
Copyright © 1989 by The Histochemical Society
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Barker, M. Weinfeld, J. Zheng, L. Li, and D. Murray Identification of Mammalian Proteins Cross-linked to DNA by Ionizing Radiation J. Biol. Chem., October 7, 2005; 280(40): 33826 - 33838. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. R. Pendleton and C. E. Machamer Infectious Bronchitis Virus 3a Protein Localizes to a Novel Domain of the Smooth Endoplasmic Reticulum J. Virol., May 15, 2005; 79(10): 6142 - 6151. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. D. Shnyder and M. J. Hubbard ERp29 Is a Ubiquitous Resident of the Endoplasmic Reticulum with a Distinct Role in Secretory Protein Production J. Histochem. Cytochem., April 1, 2002; 50(4): 557 - 566. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. R. Tobler, L. Notterpek, R. Naef, V. Taylor, U. Suter, and E. M. Shooter Transport of Trembler-J Mutant Peripheral Myelin Protein 22 Is Blocked in the Intermediate Compartment and Affects the Transport of the Wild-Type Protein by Direct Interaction J. Neurosci., March 15, 1999; 19(6): 2027 - 2036. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. C. Edwards A novel p64-related Cl- channel: subcellular distribution and nephron segment-specific expression Am J Physiol Renal Physiol, March 1, 1999; 276(3): F398 - F408. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. B. Cole, J. Ellenberg, J. Song, D. DiEuliis, and J. Lippincott-Schwartz Retrograde Transport of Golgi-localized Proteins to the ER J. Cell Biol., January 12, 1998; 140(1): 1 - 15. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Glover, T. Bayburt, M. Jonas, E. Chi, and M. H. Gelb Translocation of the 85-kDa Phospholipase A[IMAGE] from Cytosol to the Nuclear Envelope in Rat Basophilic Leukemia Cells Stimulated with Calcium Ionophore or IgE/Antigen J. Biol. Chem., June 23, 1995; 270(25): 15359 - 15367. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Velez-Granell, A. Arias, J. Torres-Ruiz, and M Bendayan Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60 and hsp70 in distinct compartments along the secretory pathway of the acinar cells J. Cell Sci., January 3, 1994; 107(3): 539 - 549. [Abstract] [PDF]
|
|
| Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact |