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Matrix metalloproteinases (MMP) are a family of endopeptidases involved in the breakdown of extracellular matrix (ECM) during both normal physiological and disease processes. MMP-2 is a zinc-dependent family member that selectively cleaves collagen and elastin, major structural components of the basement membrane. In addition, MMP-2 has been found to affect a number of non-matrix proteins such as big endothelin-1 (Fernandez-Patron et al., 1999), KISS (Takino et al., 2003), GSK3B (Kandasamy et al., 2009), and CHUK (Olivotto et al., 2013).

WD repeat domain phosphoinositide-interacting protein 1 (WIPI) is involved in the lysosomal degradation of cytoplasmic components during starvation-induced autophagy. WIPI1 is a seven bladed beta-propeller protein that provides a scaffold for the assembly of multimeric protein complexes (1). During the assembly of the autophagosome WIPI1 interacts with the lipid phosphatidylinositol-3 phosphate (PI3P) and mediates the recruitment of the large multimeric complex of ATG12-ATG5-ATG16 (1).