The TITAN5 Gene of Arabidopsis Encodes a Protein Related to the ADP Ribosylation Factor Family of GTP Binding Proteins

2000 ◽  
Vol 12 (8) ◽  
pp. 1379
Author(s):  
John McElver ◽  
David Patton ◽  
Michael Rumbaugh ◽  
Chun-ming Liu ◽  
Li Jun Yang ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Adp Ribosylation ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Adp Ribosylation Factor

scholarly journals The TITAN5 Gene of Arabidopsis Encodes a Protein Related to the ADP Ribosylation Factor Family of GTP Binding Proteins

2000 ◽  
Vol 12 (8) ◽  
pp. 1379-1392 ◽  
Author(s):  
John McElver ◽  
David Patton ◽  
Michael Rumbaugh ◽  
Chun-ming Liu ◽  
Li Jun Yang ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Adp Ribosylation ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Adp Ribosylation Factor

scholarly journals Redistribution of ADP-ribosylation factor during stimulation of permeabilized cells with GTP analogues

1991 ◽  
Vol 275 (3) ◽  
pp. 639-644 ◽  
Author(s):  
R Regazzi ◽  
S Ullrich ◽  
R A Kahn ◽  
C B Wollheim
Keyword(s):  
Insulin Secretion ◽  
Molecular Mass ◽  
Binding Proteins ◽  
Secretory Granules ◽  
Rinm5f Cells ◽  
Permeabilized Cells ◽  
Adp Ribosylation ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Adp Ribosylation Factor

Low-molecular-mass GTP-binding proteins of the ras family were analysed by [32P]GTP binding after PAGE and transfer to nitrocellulose membranes. By this technique, several GTP-binding proteins in the 20-30 kDa range were detected in both cytosolic and microsomal fractions of RINm5F cells. One of these, displaying an apparent molecular mass of about 20 kDa and a pI of 6.7, was mainly cytosolic and was shown to be the ADP-ribosylation factor (ARF) by using specific antibodies. When permeabilized RINm5F cells were incubated with the stable GTP analogues guanosine 5′-[gamma-thio]triphosphate (GTP[S]) and guanosine 5′-[beta gamma-imido]triphosphate (p[NH]ppG) the amount of ARF increased in a fraction containing both Golgi and plasma-membrane markers, but not in the fraction containing secretory granules, mitochondria and lysosomes. GTP, GDP and its beta-thio analogue did not enhance ARF binding to membranes, smg25/rab3 and rho, as well as all the other small GTP-binding proteins detected by the [32P]GTP binding, did not redistribute under these conditions. As GTP[S] stimulates insulin secretion in these cells, we also examined the relationship between ARF translocation and insulin secretion. Both phenomena were elicited by GTP[S] with an EC50 (median effective concentration) of about 10 microM. p[NH]ppG was equipotent with GTP[S] in inducing insulin secretion (EC50 about 10 microM), but higher concentrations (about 500 microns) were required to achieve the same maximal ARF redistribution. These results suggest that: (1) ARF is subject to cycling between a membrane-associated and a free/loosely attached form, determined by the species of bound guanine nucleotide; (2) ARF alone does not seem to regulate exocytosis in insulin-secreting cells.

scholarly journals ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissues.

1994 ◽  
Vol 269 (29) ◽  
pp. 18937-18942 ◽  
Author(s):  
M.M. Cavenagh ◽  
M. Breiner ◽  
A. Schurmann ◽  
A.G. Rosenwald ◽  
T. Terui ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Rat Tissues ◽  
Adp Ribosylation ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Adp Ribosylation Factor

scholarly journals Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins

1991 ◽  
Vol 266 (4) ◽  
pp. 2606-2614 ◽  
Author(s):  
R A Kahn ◽  
F G Kern ◽  
J Clark ◽  
E P Gelmann ◽  
C Rulka
Keyword(s):  
Binding Proteins ◽  
Adp Ribosylation ◽  
Gtp Binding Proteins ◽  
Gtp Binding
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