Different ARF domains are required for the activation of cholera toxin and phospholipase D.

@article{citeulike:3041057, abstract = {ADP-ribosylation factors (ARFs), initially described as activators of cholera toxin ADP-ribosyltransferase activity, regulate intracellular vesicular membrane trafficking and stimulate a phospholipase D (PLD) isoform. ARF-like (ARL) proteins are structurally related to ARFs but do not activate cholera toxin and have relatively little effect on PLD. A new human ARL gene termed hARL1, which shares 57\% amino acid identity with hARF1, was identified using a polymerase chain reaction-based cloning method. To determine whether different structural elements are responsible for the activation structural elements are responsible for the activation of the A subunit of cholera toxin and PLD, chimeric proteins were constructed by switching the amino-terminal 73 amino acids of ARF1 and ARL1. The recombinant rL73/F protein, in which the amino-terminal 73 amino acids of ARL1 replaced those of ARF1, activated the A subunit of cholera toxin, whereas the rF73/L protein, in which the NH2-terminal 73 amino acids of ARF1 replaced those of ARL1, was inactive. The two chimeric proteins had quite opposite effects on PLD activity. rF73/L activated PLD as effectively as rARF1, whereas rL73/F protein activated PLD only slightly. It appears that the amino-terminal region of ARF1 is not critical for its action as a GTP-dependent activator of cholera toxin, whereas it is necessary for activation of the putative effector enzyme, PLD.}, address = {Pulmonary-Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.}, author = {Zhang, G. F. and Patton, W. A. and Lee, F. J. and Liyanage, M. and Han, J. S. and Rhee, S. G. and Moss, J. and Vaughan, M. }, citeulike-article-id = {3041057}, issn = {0021-9258}, journal = {The Journal of biological chemistry}, keywords = {arf, nt}, month = {January}, number = {1}, pages = {21--24}, posted-at = {2008-07-24 20:18:08}, priority = {2}, title = {Different ARF domains are required for the activation of cholera toxin and phospholipase D.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/7814376}, volume = {270}, year = {1995} }

TY - JOUR ID - citeulike:3041057 L3 - citeulike-article-id:3041057 TI - Different ARF domains are required for the activation of cholera toxin and phospholipase D. JF - The Journal of biological chemistry VL - 270 IS - 1 SP - 21 EP - 24 AD - Pulmonary-Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892. SN - 0021-9258 N2 - ADP-ribosylation factors (ARFs), initially described as activators of cholera toxin ADP-ribosyltransferase activity, regulate intracellular vesicular membrane trafficking and stimulate a phospholipase D (PLD) isoform. ARF-like (ARL) proteins are structurally related to ARFs but do not activate cholera toxin and have relatively little effect on PLD. A new human ARL gene termed hARL1, which shares 57% amino acid identity with hARF1, was identified using a polymerase chain reaction-based cloning method. To determine whether different structural elements are responsible for the activation structural elements are responsible for the activation of the A subunit of cholera toxin and PLD, chimeric proteins were constructed by switching the amino-terminal 73 amino acids of ARF1 and ARL1. The recombinant rL73/F protein, in which the amino-terminal 73 amino acids of ARL1 replaced those of ARF1, activated the A subunit of cholera toxin, whereas the rF73/L protein, in which the NH2-terminal 73 amino acids of ARF1 replaced those of ARL1, was inactive. The two chimeric proteins had quite opposite effects on PLD activity. rF73/L activated PLD as effectively as rARF1, whereas rL73/F protein activated PLD only slightly. It appears that the amino-terminal region of ARF1 is not critical for its action as a GTP-dependent activator of cholera toxin, whereas it is necessary for activation of the putative effector enzyme, PLD. KW - arf KW - nt AU - Zhang, GF AU - Patton, WA AU - Lee, FJ AU - Liyanage, M AU - Han, JS AU - Rhee, SG AU - Moss, J AU - Vaughan, M PY - 1995/01/06/ UR - http://view.ncbi.nlm.nih.gov/pubmed/7814376 ER -