The activation loop of phosphatidylinositol phosphate kinases determines signaling specificity.

By J. Kunz, Monita P. Wilson, Marina V. Kisseleva, James H. Hurley, P. Majerus, R. Anderson. 2000

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PIP4Ks Suppress Insulin Signaling through a Catalytic-Independent Mechanism (2018, unknown): “…of PIP4Ks have been inconsistent, recent global quantitative mapping of protein subcellular localization suggests that both PIP5Ks and PIP4Ks are largely bound to plasma membranes (Bultsma et al., 2010; Hinchliffe et al., 1999, 2002; Itoh et al., 1998; Itzhak et al., 2016; Kunz et al., 2000).”
The emerging field of lipidomics (2005, background): “' INTERFACIAL CATALYSIS ' requires selective targeting and binding of the enzyme to the lipid surface and effective substrate recognitio”
Phosphatidylinositol 5-phosphate 4-kinase (PIP4K) regulates TOR signaling and cell growth during Drosophila development (2013, background): “Inspection of the region corresponding to the “activation loop” (20) whose sequence is reported to correlate with PIP5K versus PIP4K activity (13) suggests that CG17471 encodes a PIP4K activity (Fig.”
Phosphoinositides: tiny lipids with giant impact on cell regulation. (2013, background): “The substrate specificity of the enzymes is determined by the activation loop within their catalytic domains and can be reversed by swapping activation loops between the type I and type II forms (832).”