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A more recent version of this article appeared on July 12, 2002
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Papers In Press, published online ahead of print May 8, 2002
J. Biol. Chem, 10.1074/jbc.M110814200
Submitted on November 12, 2001
Revised on May 2, 2002
Accepted on May 8, 2002

Intracellular processing of metalloprotease disintegrin ADAM12

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

Biochemistry, Kansas State University, Manhattan, KS 66506

Corresponding Author: zolkiea{at}ksu.edu

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 to the cell surface has been questioned. In this report, we show that the full length ADAM12 is N-glycosylated in the endoplasmic reticulum (ER) and proteolytically processed in the trans-Golgi to a ~90-kDa form. The ~90-kDa form, which lacks the prodomain, is the predominant form present at the cell surface. Replacement of Leu73 in the putativeƒnalpha -helical region in the prodomain with a proline results in retention of ADAM12 in the ER and a complete lack of its processing. Deletion of the entire pro- and metalloprotease domains, however, does not affect the processing and trafficking of ADAM12. In contrast, replacement of the cytoplasmic domain of ADAM12 with that of ADAM9 or adding the c-myc tag at the C-terminus leads to a significant increase of 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 a 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.


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