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The ADP-ribosylation factor (Arf) family of small GTP-binding proteins regulate many cellular events by cycling between active GTP- and inactive GDP-bound forms. They depend on GTP-exchange factors (GEFs) for activation and GTPase-activating proteins (GAPs) for inactivation (Donaldson and Jackson 2011). Mammalian cells express six ARF isoforms (ARF1–ARF6), ARF1 and ARF6 are the best characterized. ARF1 regulates the membrane trafficking mainly at the Golgi, whereas ARF6 regulates endocytosis, exocytosis, and actin reorganization at the plasma membrane (Donaldson and Jackson 2011).
In the human genome, more than 30 genes are predicted to encode proteins with an ARF-GAP domain that have been classified into ten subfamilies on the basis of sequence similarities of their ARF-GAP domains (Kahn et al. 2008). The ARF GAP with dual pleckstrin homology (PH) domains (ADAP) subfamily...
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Robinson, C.R., Kanamarlapudi, V. (2018). ADAP2. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101964
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DOI: https://doi.org/10.1007/978-3-319-67199-4_101964
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