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A more recent version of this article appeared on May 9, 2003
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M211448200v1
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Papers In Press, published online ahead of print March 13, 2003
J. Biol. Chem, 10.1074/jbc.M211448200
Submitted on November 10, 2002
Revised on March 13, 2003
Accepted on March 13, 2003

Bone morphogenetic protein (BMP)-1: identification of the minimal domain structure for C-proteinase activity

Nichola Hartigan, Laure Garrigue-Antar, and Karl E. Kadler

School of Biological Sciences, University of Manchester, Manchester, UK M13 9PT

Corresponding Author: karl.kadler{at}man.ac.uk

Bone morphogenetic protein (BMP)-1 is a shorter spliced variant of mammalian tolloid (mTld), both of which cleave the C-propeptides of type I procollagen during the synthesis of extracellular matrix collagen fibrils. The fact that BMP-1 and mTld both exhibit procollagen C-proteinase (PCP) activity and that BMP-1 is the smaller variant, might indicate that BMP-1 comprises the minimal required sequences for PCP activity. BMP-1 comprises a metalloproteinase domain, 3 CUB domains, and an EGF-like domain, which is located between the second and third CUB domains. In this study we showed that; 1) the CUB1 domain is required for secretion of the molecule. Domain swapping experiments, in which CUB1 and other CUB domains were interchanged, resulted in retention of the proteins by cells. Therefore, CUB1 and its location immediately adjacent to the metalloproteinase domain are essential for secretion of the protein; 2) mutants lacking the EGF-like and CUB3 domains exhibited full C-proteinase activity. In contrast, mutants lacking the CUB2 domain were poor C-proteinases; 3) Further studies showed that E483 on the b4-b5 loop of CUB2 is essential for C-proteinase activity of BMP-1. In conclusion, the study showed that the minimal domain structure for PCP activity is considerably shorter than expected and comprises the metalloproteinase domain, and the CUB1 and CUB2 domains of BMP-1.


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