JBC GenomeOne product landing page

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Falk, M. M.
Right arrow Articles by Gilula, N. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Falk, M. M.
Right arrow Articles by Gilula, N. B.

J Biol Chem, Vol. 273, Issue 14, 7856-7864, April 3, 1998

Connexin Membrane Protein Biosynthesis Is Influenced by Polypeptide Positioning within the Translocon and Signal Peptidase Access

Matthias M. Falk and Norton B. Gilula

From the Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037

We reported previously (Falk, M. M., Kumar, N. M., and Gilula, N. B. (1994) J. Cell Biol. 127, 343-355) that the membrane integration of polytopic connexin polypeptides can be accompanied by an inappropriate cleavage that generates amino-terminal truncated connexins. While this cleavage was not detected in vivo, translation in standard cell-free translation/translocation systems resulted in the complete cleavage of all newly integrated connexins. Partial cleavage occurred in heterologous expression systems that correlated with the expression level. Here we report that the transmembrane topology of connexins generated in microsomal membranes was identical to the topology of functional connexins in plasma membranes. Characterization of the cleavage site and reaction showed that the connexins were processed by signal peptidase immediately downstream of their first transmembrane domain in a reaction similar to the removal of signal peptides from pre-proteins. Increasing the length and hydrophobic character of the signal anchor sequence of connexins completely prevented the aberrant cleavage. This result indicates that their signal anchor sequence was falsely recognized and positioned as a cleavable signal peptide within the endoplasmic reticulum translocon, and that this mispositioning enabled signal peptidase to access the cleavage sites. The results provide direct evidence for the involvement of unknown cellular factors in the membrane integration process of connexins.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
T. Thomas, K. Jordan, J. Simek, Q. Shao, C. Jedeszko, P. Walton, and D. W. Laird
Mechanisms of Cx43 and Cx26 transport to the plasma membrane and gap junction regeneration
J. Cell Sci., October 1, 2005; 118(19): 4451 - 4462.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. Roscoe, G. I. L. Veitch, X.-Q. Gong, E. Pellegrino, D. Bai, E. McLachlan, Q. Shao, G. M. Kidder, and D. W. Laird
Oculodentodigital Dysplasia-causing Connexin43 Mutants Are Non-functional and Exhibit Dominant Effects on Wild-type Connexin43
J. Biol. Chem., March 25, 2005; 280(12): 11458 - 11466.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Locke, I. V. Koreen, J. Y. Liu, and A. L. Harris
Reversible Pore Block of Connexin Channels by Cyclodextrins
J. Biol. Chem., May 28, 2004; 279(22): 22883 - 22892.
[Abstract] [Full Text] [PDF]

Home page
 Cardiovasc ResHome page
P. E.M. Martin and W.H. Evans
Incorporation of connexins into plasma membranes and gap junctions
Cardiovasc Res, May 1, 2004; 62(2): 378 - 387.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
V. Lagree, K. Brunschwig, P. Lopez, N. B. Gilula, G. Richard, and M. M. Falk
Specific amino-acid residues in the N-terminus and TM3 implicated in channel function and oligomerization compatibility of connexin43
J. Cell Sci., August 1, 2003; 116(15): 3189 - 3201.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
J. B. Dean, D. Ballantyne, D. L. Cardone, J. S. Erlichman, and I. C. Solomon
Role of gap junctions in CO2 chemoreception and respiratory control
Am J Physiol Lung Cell Mol Physiol, October 1, 2002; 283(4): L665 - L670.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
C. M. Ott and V. R. Lingappa
Integral membrane protein biosynthesis: why topology is hard to predict
J. Cell Sci., May 15, 2002; 115(10): 2003 - 2009.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
J. K. VanSlyke and L. S. Musil
Dislocation and degradation from the ER are regulated by cytosolic stress
J. Cell Biol., April 29, 2002; 157(3): 381 - 394.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
M. Falk
Connexin-specific distribution within gap junctions revealed in living cells
J. Cell Sci., January 11, 2000; 113(22): 4109 - 4120.
[Abstract] [PDF]

Home page
 Circ. Res.Home page
D. C. Spray
Gap Junction Proteins : Where They Live and How They Die
Circ. Res., September 21, 1998; 83(6): 679 - 681.
[Full Text]

Home page
 J. Cell Biol.Home page
J. K. VanSlyke and L. S. Musil
Dislocation and degradation from the ER are regulated by cytosolic stress
J. Cell Biol., April 29, 2002; 157(3): 381 - 394.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.