|Table of Contents|

Matrix Metalloproteinase-14 Inhibits the Activity of Bst-2 viaTheir Cytoplasmic Domains Dependent Interaction(PDF)

《南京师大学报（自然科学版）》[ISSN:1001-4616/CN:32-1239/N]

Issue:
2016年03期
Page:
79-
Research Field:
·生命科学·
Publishing date:

Info

Title:
Matrix Metalloproteinase-14 Inhibits the Activity of Bst-2 viaTheir Cytoplasmic Domains Dependent Interaction
Author(s):
Fan Long; Zhu Cuicui; Pi Yurui; Wu Zhaomeng; Lu Shan; Liu Ping
School of Life Sciences，Nanjing Normal University，Nanjing 210023，China
Keywords:
Bst-2; MT1-MMP; virus release
PACS:
Q291
DOI:
10.3969/j.issn.1001-4616.2016.03.014
Abstract:
Bst-2（bone marrow stromal cell antigen 2）is a type II membrane protein and acts as a tetherin to inhibit virion releasing from infectious cells. Membrane type-1 matrix metalloproteinase（MT1-MMP）is a protease and plays a pivotal role in cellular growth and migration by activating proMMP-2 into active MMP2. In this study，we explored the molecular mechanism of MT1-MMP inhibiting the activity of Bst-2. From experimental data，it’s elaborated that MT1-MMP inhibited the tetherin activity of Bst-2 via the interaction within，and the cytoplasmic domains of both Bst-2 and MT1-MMP play critical roles in the interaction. Furthermore，we found that that N-terminal domain of Bst-2 is not only important in relating to the activity of Bst-2 itself，but important for inhibiting the activities of MT1-MMP and 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 indicate that both N-terminal domain of Bst-2 and C-terminal domain of MT1-MMP are crucial in their activity down-regulation.

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Last Update: 2016-09-30