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Int. J. Mol. Sci. 2016, 17(6), 818; doi:10.3390/ijms17060818

MT1-MMP Inhibits the Activity of Bst-2 via Their Cytoplasmic Domains Dependent Interaction

1,†
,
2,†
,
1
,
3
,
1
and
1,*
1
Jiangsu Province Key Laboratory for Molecular and Medicine Biotechnology, College of Life Sciences, Nanjing Normal University, Nanjing 210023, China
2
Laboratory of Molecular Biology, Jiangsu Province Hospital of Traditional Chinese Medicine, Nanjing 210029, China
3
Department of Urology, Jiangsu Province Hospital of Traditional Chinese Medicine, Nanjing 210029, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Masatoshi Maki
Received: 14 February 2016 / Revised: 12 May 2016 / Accepted: 16 May 2016 / Published: 26 May 2016
(This article belongs to the Special Issue Metalloproteins)
View Full-Text   |   Download PDF [2616 KB, uploaded 26 May 2016]   |  

Abstract

Bst-2 (bone marrow stromal cell antigen 2) is a type II membrane protein, and it acts as a tetherin to inhibit virion releasing from infectious cells. Membrane type-1 matrix metalloproteinase (MT1-MMP) is a protease. It plays a pivotal role in cellular growth and migration by activating proMMP-2 into active MMP2. Our results here elaborate that MT1-MMP inhibits the tetherin activity of Bst-2 by interacting with Bst-2, and the cytoplasmic domains of both Bst-2 and MT1-MMP play critical roles within this interaction. Based on our experimental data, the assays for virion release and co-immunoprecipitation have clearly demonstrated that the activity of Bst-2 is markedly inhibited by MT1-MMP via their interaction; and both the N-terminal domain of Bst-2 and the C-terminal domain of MT1-MMP are important in the interaction. Immunostaining and Confocal Microscopy assay shows that MT1-MMP interacts with Bst-2 to form granular particles trafficking into cytoplasm from membrane and, finally, results in Bst-2 and MT1-MMP both being inhibited. In addition, mutant experiments elucidate that the N-terminal domain of Bst-2 is not only important in relating to the activity of Bst-2 itself, but is important for inhibiting the MT1-MMP/proMMP2/MMP2 pathway. These findings suggest that MT1-MMP is a novel inhibitor of Bst-2 in MT1-MMP expressed cell lines and also indicate that both the N-terminal domain of Bst-2 and the C-terminal domain of MT1-MMP are crucial in down-regulation. View Full-Text
Keywords: bone marrow stromal cell antigen 2 (Bst-2); Membrane type-1 matrix metalloproteinase (MT1-MMP); virus release; tetherin bone marrow stromal cell antigen 2 (Bst-2); Membrane type-1 matrix metalloproteinase (MT1-MMP); virus release; tetherin
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MDPI and ACS Style

Fan, L.; Liu, L.; Zhu, C.; Zhu, Q.; Lu, S.; Liu, P. MT1-MMP Inhibits the Activity of Bst-2 via Their Cytoplasmic Domains Dependent Interaction. Int. J. Mol. Sci. 2016, 17, 818.

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