Journal
TRENDS IN CELL BIOLOGY
Volume 29, Issue 1, Pages 6-19Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2018.08.006
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Funding
- Deutsche Forschungsgemeinschaft [KR2047/1-2, KR2047/1-3, KR2047/3-1]
- Wilhelm-Sander-Stiftung [2016.040.1]
- European Union Seventh Framework Programme [FP7/2007-2013 263307]
- Princess Margaret Postdoctoral Excellence Fellowship
- European Molecular Biology Organization [ALTF 116-2018]
- Alexander von Humboldt Foundation [DEU 1199182 FLF-P]
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Tissue inhibitor of metalloproteinase 1 (TIMP-1) is a major player in preserving tissue integrity and has recently also emerged as a decisive factor in several human pathologies. This appreciation has prompted this review addressing the largely underestimated complexity of the functions executed by TIMP-1 and their mechanistic basis. In fact, the versatile impact of TIMP-1 on cellular functions stems from its two-domain structure harboring metalloproteinase-inhibitory and cytokine-like signaling activities. This feature leads to functional interactions with numerous and distinct enzymatic and cell-surface proteins that initiate an exceptionally broad range of downstream effects. We propose here that this multifunctionality and the remarkably large interactome explain the diverse biological consequences of TIMP-1 expression in health and disease.
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