ZFYVE1, also termed double FYVE-containing protein 1 (DFCP1) is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. It plays a role in the formation of lipid droplets (LDs), regulating their morphology, size and distribution which are storage organelles, central to lipid and energy homeostasis [, ].ZFYVE1 harbors two B-box domains, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterised by a C6H2 zinc-binding consensus motif [, , , ].
This entry represents the first BBox type 1 domain of ZFYVE1.ZFYVE1, also termed double FYVE-containing protein 1 (DFCP1) is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. It plays a role in the formation of lipid droplets (LDs), regulating their morphology, size and distribution which are storage organelles, central to lipid and energy homeostasis [, ].ZFYVE1 harbors two B-box domains, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterised by a C6H2 zinc-binding consensus motif [, , , ].
This entry represents the second BBox-type 1 domain of ZFYVE1.ZFYVE1, also termed double FYVE-containing protein 1 (DFCP1) is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYVE1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by Wortmannin, a PI3-kinase inhibitor. It plays a role in the formation of lipid droplets (LDs), regulating their morphology, size and distribution which are storage organelles, central to lipid and energy homeostasis [, ].ZFYVE1 harbors two B-box domains, both of which show high sequence similarity with B-Box-type 1 zinc finger found in tripartite motif-containing proteins (TRIMs). The type 1 B-box (Bbox1) zinc finger is characterised by a C6H2 zinc-binding consensus motif [, , , ].
