High impact information on ARF1A1c

• GNOM is a membrane-associated guanine-nucleotide exchange factor on ADP-ribosylation factor G protein (ARF GEF) [1].
• Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal cell polarity [2].
• Core components of the vesicle transport machinery, such as ADP-ribosylation factor (ARF) GTPases, have been studied primarily at the single-cell level [2].
• Our results suggest that Cyp5 may regulate the ARF GEF function of the GNOM protein during embryogenesis [3].
• Co-expression of a membrane-bound reporter protein containing the FAD2 C-terminus with a dominant-negative mutant of ADP-ribosylation factor (Arf)1 abolished transient localization of the reporter protein in the Golgi, indicating that the FAD2 peptide signal acts as an ER retrieval motif [4].

Biological context of ARF1A1c

• The level of ARF mRNA was found to be nearly constant during all cell growth stages in suspension cultures [5].
• The predicted amino acid sequence was highly homologous to the known yeast, bovine and human ARF sequences [5].
• A cDNA clone encoding a small GTP-binding protein, the ADP-ribosylation factor (ARF) was isolated from a cDNA library of Arabidopsis thaliana cultured cells [5].

Other interactions of ARF1A1c

• Several other proteins were also identified by in vitro GTP binding, including Arabidopsis and tobacco homologues of Rab11, ARF (ADP-ribosylation factor) and Sar proteins, as well as a novel 22 kDa Arabidopsis protein (ATG81) [6].

References