Amot Recognizes a Juxtanuclear Endocytic Recycling Compartment via a Novel Lipid Binding Domain

Rab13-dependent Trafficking of RhoA Is Required for Directional Migration and Angiogenesis

“…Based on in vitro experiments with synthetic lipid membranes, a recent study attributed liposome tubulation activity to a region in the amino terminus of Amot (41). Although our findings also indicate that Amot structures intracellular membranes, we observed that amot Ϫ/Ϫ ECs contained numerous Rab13-associated tubular structures (Fig.…”

“…Mupp1, which binds Syx directly (18,39), cross-links Syx to Amot (39,40). Because Amot has a lipidbinding domain that favors mono-over di-or tri-phosphorylated phosphatidylinositols (41), it could recruit Mupp1 and Syx to vesicles. The colocalization of Amot with Syx (Fig.…”

The Amotl2 Gene Inhibits Wnt/β-Catenin Signaling and Regulates Embryonic Development in Zebrafish

“…Amotl2 Is Localized in Recycling Endosomes-A previous report demonstrates that AMOT is localized in endocytic recycling compartments through the coiled-coil domain (41). We asked whether the Amotl2-containing cytosolic punctuate structures are also recycling compartments.…”

C2 domain membrane penetration by group IVA cytosolic phospholipase A2 induces membrane curvature changes

“…2 ). The ENTH, BAR, and ACCH domains insert into the hydrocarbon region of the membrane bilayer, which is a prerequisite for their ability to induce membrane curvature changes ( 31,(37)(38)(39). To test if hydrophobic and aromatic residues, which typically insert into membranes, were required for liposome morphology changes, we prepared mutations of hydrophobic and aromatic residues in calcium binding loops 1 and 3 of the C2 domain ( Fig.…”

“…been found to induce membrane curvature changes ( 27 ), including the epsin N-terminal homology (ENTH) ( 28 ), bin-amphiphysin-Rvs167 (BAR) ( 29 ), Pleckstrin homology (PH) ( 30 ), Amot coiled-coil homology domain (ACCH) ( 31 ), and C2 domains ( 32 ). Here, we investigate the ability of the isolated C2 domain of cPLA 2 ␣ to induce changes to lipid structure.…”