%0 Journal Article
%T Recognizing the Molecular Multifunctionality and Interactome of TIMP-1.
%A Grünwald B
%A Schoeps B
%A Krüger A
%J Trends Cell Biol
%V 29
%N 1
%D 01 2019
%M 30243515
%F 21.167
%R 10.1016/j.tcb.2018.08.006
%X 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.