Recently identified lipid phosphate phosphatase-related proteins (LPPRs) are highly expressed in the central nervous system and have been implicated in axonal outgrowth, regeneration and synaptic plasticity. Five members of the LPPR family (LPPR1–LPPR5) have been identified so far, however, whether they have redundant or separate functions, and what their mechanisms of action are, remain unknown. Here (p. 3210), Herbert Geller, Panpan Yu and colleagues used affinity purification coupled to mass spectrometry to identify interaction partners of LPPR1. They found that, amongst others, LPPR1 associated with mTOR and PTEN, as well as with proteins involved in lipid biosynthesis and various other biological processes. Unexpectedly, they also discovered that LPPR1 interacted with LPPR3, LPPR4 and LPPR5. The authors then demonstrated that co-expression of LPPR1 or LPPR5 with another LPPR resulted in an increase in protein levels of co-expressed LPPRs. Overexpressed LPPR1 localised to both intracellular membrane structures and the cell surface, and induced the formation of membrane protrusions, which contained myosin X and were actin dependent. Surprisingly, co-expression of LPPRs further increased the number of LPPR-induced protrusions and the proportion of LPPRs at the plasma membrane, where they colocalised to a high extent. Thus, the findings presented in this study suggest that LPPRs function neither redundantly nor separately, but rather in a complex formed through cooperative interactions.
LPPRs band together at the plasma membrane
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LPPRs band together at the plasma membrane. J Cell Sci 1 September 2015; 128 (17): e1703. doi:
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