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Involved in Golgi to cell surface membrane traffic.
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Binding sites on Fapp1 protein for Arf1 (show ARF1 Proteins) and phosphatidylinositol-4-phosphate minimally overlap
We report the complete (1)H, (13)C and (15)N resonance assignments of the FAPP1-PH in its free state and those induced by PtdIns(4)P or detergent micelles.
Molecular basis of phosphatidylinositol 4-phosphate and ARF1 (show ARF1 Proteins) GTPase (show RACGAP1 Proteins) recognition by the FAPP1 pleckstrin (show PLEK Proteins) homology (PH) domain.
The micelle-bound structure of the FAPP1 pleckstrin (show PLEK Proteins) homology domain reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration.
Data show that FAPP1 and 2 are essential components of a phosphatidylinositol 4-phosphate- and ADP-ribosylation factor (show ARF1 Proteins)-regulated machinery that controls generation of constitutive post-Golgi carriers.
Involved in Golgi to cell surface membrane traffic. Induces membrane tubulation. Binds preferencially to phosphatidylinositol 4-phosphate (PtdIns4P) (By similarity).
pleckstrin homology domain-containing family A member 3
, PH domain-containing family A member 3
, four-phosphate-adaptor protein 1
, phosphatidylinositol-four-phosphate adapter protein 1
, phosphoinositol 4-phosphate adapter protein 1
, pleckstrin homology domain-containing, family A (phosphoinositide binding specific) member 3