JBC

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


     

Originally published In Press as doi:10.1074/jbc.M110814200 on May 8, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26403-26411, July 19, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/29/26403    most recent
M110814200v1
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 Cao, Y.
Right arrow Articles by Zolkiewska, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cao, Y.
Right arrow Articles by Zolkiewska, A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Intracellular Processing of Metalloprotease Disintegrin ADAM12*

Yi Cao, Qing Kang, Zhefeng Zhao, and Anna ZolkiewskaDagger

From the Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506

ADAM12 has been implicated in cell-cell interactions in myogenesis and cancer, but the structure of the mature form of ADAM12 is not known, and its localization on the cell surface has been questioned. In this report, we show that full-length ADAM12 is N-glycosylated in the endoplasmic reticulum (ER) and proteolytically processed in the trans-Golgi network to an ~90-kDa form. The ~90-kDa form, which lacks the prodomain, was the predominant form present at the cell surface. Replacement of Leu73 in the putative alpha -helical region in the prodomain with proline resulted in retention of ADAM12 in the ER and a complete lack of its processing. However, deletion of the entire pro- and metalloprotease domains did not affect the processing and trafficking of ADAM12. In contrast, replacement of the cytoplasmic domain of ADAM12 with that of ADAM9 or adding a c-Myc tag at the C terminus led to a significant increase in transport of the protein to the cell surface. These results suggest that the cytoplasmic domain of ADAM12 plays an important role in regulating ADAM12 exit from the ER. We conclude that properly folded mouse ADAM12, after passing a rate-limiting step of exit from the ER, is processed in the secretory pathway and reaches the cell surface, where it can mediate adhesion-mediated signaling.

* This work was supported by National Institutes of Health Grant AR45787 and COBRE Award P20 RR15563 and by matching support from the State of Kansas. This is Contribution 02-113-J from the Kansas Agricultural Experiment Station.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry, Kansas State University, 104 Willard Hall, Manhattan, KS 66506. Tel.: 785-532-3082; Fax: 785-532-7278; E-mail: zolkiea@ksu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
E. Dyczynska, D. Sun, H. Yi, A. Sehara-Fujisawa, C. P. Blobel, and A. Zolkiewska
Proteolytic Processing of Delta-like 1 by ADAM Proteases
J. Biol. Chem., January 5, 2007; 282(1): 436 - 444.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B.-H. Koo, J.-M. Longpre, R. P. T. Somerville, J. P. Alexander, R. Leduc, and S. S. Apte
Cell-surface Processing of Pro-ADAMTS9 by Furin
J. Biol. Chem., May 5, 2006; 281(18): 12485 - 12494.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
U. M. Wewer, M. Morgelin, P. Holck, J. Jacobsen, M. C. Lydolph, A. H. Johnsen, M. Kveiborg, and R. Albrechtsen
ADAM12 Is a Four-leafed Clover: THE EXCISED PRODOMAIN REMAINS BOUND TO THE MATURE ENZYME
J. Biol. Chem., April 7, 2006; 281(14): 9418 - 9422.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
J. Huang, L. C. Bridges, and J. M. White
Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members
Mol. Biol. Cell, October 1, 2005; 16(10): 4982 - 4991.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
P. Lafuste, C. Sonnet, B. Chazaud, P. A. Dreyfus, R. K. Gherardi, U. M. Wewer, and F.-J. Authier
ADAM12 and {alpha}9{beta}1 Integrin Are Instrumental in Human Myogenic Cell Differentiation
Mol. Biol. Cell, February 1, 2005; 16(2): 861 - 870.
[Abstract] [Full Text] [PDF]

Home page
 DevelopmentHome page
A. Sapir, E. Assa-Kunik, R. Tsruya, E. Schejter, and B.-Z. Shilo
Unidirectional Notch signaling depends on continuous cleavage of Delta
Development, January 1, 2005; 132(1): 123 - 132.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Roy, U. M. Wewer, D. Zurakowski, S. E. Pories, and M. A. Moses
ADAM 12 Cleaves Extracellular Matrix Proteins and Correlates with Cancer Status and Stage
J. Biol. Chem., December 3, 2004; 279(49): 51323 - 51330.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Sundberg, C. K. Thodeti, M. Kveiborg, C. Larsson, P. Parker, R. Albrechtsen, and U. M. Wewer
Regulation of ADAM12 Cell-surface Expression by Protein Kinase C {epsilon}
J. Biol. Chem., December 3, 2004; 279(49): 51601 - 51611.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Pathol.Home page
T. Kodama, E. Ikeda, A. Okada, T. Ohtsuka, M. Shimoda, T. Shiomi, K. Yoshida, M. Nakada, E. Ohuchi, and Y. Okada
ADAM12 Is Selectively Overexpressed in Human Glioblastomas and Is Associated with Glioblastoma Cell Proliferation and Shedding of Heparin-Binding Epidermal Growth Factor
Am. J. Pathol., November 1, 2004; 165(5): 1743 - 1753.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
Y. Cao, Z. Zhao, J. Gruszczynska-Biegala, and A. Zolkiewska
Role of Metalloprotease Disintegrin ADAM12 in Determination of Quiescent Reserve Cells during Myogenic Differentiation In Vitro
Mol. Cell. Biol., October 1, 2003; 23(19): 6725 - 6738.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Chesneau, J. D. Becherer, Y. Zheng, H. Erdjument-Bromage, P. Tempst, and C. P. Blobel
Catalytic Properties of ADAM19
J. Biol. Chem., June 13, 2003; 278(25): 22331 - 22340.
[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 © 2002 by the American Society for Biochemistry and Molecular Biology.