Abstract
The Angiomotin (Amot) family of adaptor proteins binds core polarity proteins involved in polarization of the apical membrane and transcriptional co-activators as a regulator of cell growth and migration. The Amot coiled-coil homology (ACCH) domain has the unique property to selectively bind monophosphorylated phosphatidylinositols (PI) in a similar manner as FYVE, PX and PH domains. We endeavored to understand the physical properties of these PI containing membranes as an interface between the ACCH domain and the lipidic environment for membrane association. As a result, we suggest that the presence of the PI lipid induces a phase separation thereby creating an enriched nano- to micro- scaled ordered lipid domain. It is under this context that we then are able to discuss ACCH domain activity as a function of lipid content, as well as further design assays to ascertain the contributions of selected lysines and arginines toward lipid head-group binding.This work was supported by NIH K01CA169078-01, NSF DSRP-IUPUI, NSF Bridges to the Baccalaureate IUPUI, NSF UROP-IUPUI, IUPUI Project Seed, IUSM LHSI and NSF LSAMP-IUPUI.
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