The amino terminus of ADP-ribosylation factor (ARF) 1 is essential for interaction with Gs and ARF GTPase-activating protein.

Randazzo, Paul A.; Terui, Takeshi; Sturch, Stacey; Kahn, Richard

doi:10.1016/s0021-9258(18)43906-3

Cited by 58 publications

(23 citation statements)

References 21 publications

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“…Other activities ascribed to Arf proteins include cofactor for cholera toxin (5, 6) and regulator of coat protein binding to membranes (7,8). In addition to the regulatory ligand GTP, Arf activities require an intact amino terminus (9,10) and the cotranslational covalent addition of myristate to the amino-terminal glycine (3,7,(11)(12)(13)(14).…”

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confidence: 99%

“…Based on data from previous studies, the N-terminal domain of Arf has been implicated as an effector domain. Deletion of the N-terrninal 13 or 17 amino acids results in proteins that can bind GTP but that are inactive as cofactors for cholera toxin-catalyzedADP-ribosylation of'G, (9,10). These mutant proteins also have decreased affinity for Arf GTPase-activating protein (10).…”

mentioning

confidence: 99%

“…Deletion of the N-terrninal 13 or 17 amino acids results in proteins that can bind GTP but that are inactive as cofactors for cholera toxin-catalyzedADP-ribosylation of'G, (9,10). These mutant proteins also have decreased affinity for Arf GTPase-activating protein (10). Thus, the N terminus meets one of the criteria used to define the effector domain in Ras.…”

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confidence: 99%

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The Myristoylated Amino Terminus of ADP-ribosylation Factor 1 Is a Phospholipid- and GTP-sensitive Switch

Randazzo

Terui

Sturch

et al. 1995

Journal of Biological Chemistry

135

129

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ADP-ribosylation factor 1 (Arf1) is an essential N-myristoylated 21-kDa GTP-binding protein with activities that include the regulation of membrane traffic and phospholipase D activity. Both the N terminus of the protein and the N-myristate bound to glycine 2 have previously been shown to be essential to the function of Arf in cells. We show that the bound nucleotide affects the conformation of either the N terminus or residues of Arf1 that are in direct contact with the N terminus. This was demonstrated by examining the effects of mutations in this N-terminal domain on guanosine 5'-O-(3-thio)triphosphate (GTP gamma S) and GDP binding and dissociation kinetics. Arf1 mutants, lacking 13 or 17 residues from the N terminus or mutated at residues 3-7, had a greater affinity for GTP gamma S and a lower affinity for GDP than did the wild-type protein. As the N terminus is required for interactions with target proteins, we conclude that the N terminus of Arf1 is a GTP-sensitive effector domain. When Arf1 was acylated, the GTP-dependent conformational changes were codependent on added phospholipids. In the absence of phospholipids, myristoylated Arf1 has a lower affinity for GTP gamma S than for GDP, and in the presence of phospholipids, the myristoylated protein has a greater affinity for GTP gamma S than for GDP. Thus, N-myristoylation is a critical component in the construction of this phospholipid- and GTP-dependent switch.

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confidence: 99%

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confidence: 99%

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The Myristoylated Amino Terminus of ADP-ribosylation Factor 1 Is a Phospholipid- and GTP-sensitive Switch

Randazzo

Terui

Sturch

et al. 1995

Journal of Biological Chemistry

135

129

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“…Residue 1 of Arf1 corresponds to residue 3 of NtArl8 and thus, the first two residues of the first b strand are missing in D17Arf1 (Figure S1), which may destabilize the GTP-like form of D17Arf1-GDP. Notably, considerable differences in the GDP dissociation rate constants for D13Arf1 and D17Arf1 have been measured (Randazzo et al, 1994(Randazzo et al, , 1995, and, as mentioned above, the concentration of Mg 2+ also affects the transition rates more drastically for Arf1 than it does for NtArl8.…”

Section: Structurementioning

confidence: 90%

“…Many Arf-family proteins are myristoylated at the highly conserved position 2 Gly (see Figure S1 available online), and the N-terminal region, including the helix, participates in membrane association/dissociation events that are initiated by a bound nucleotide (Kahn et al, 1992). Additionally, N-terminal modifications, e.g., myristoylation and truncation of the helix alter the apparent GDP to GTP exchange rate constant, which affects the bound nucleotide equilibrium population (Randazzo et al, 1994(Randazzo et al, , 1995Franco et al, 1995). Finally, Mg 2+ , which is found in the GTP form and, in many cases, also in the GDP form (Figure 1), alters the GDP to GTP exchange rate constant (Franco et al, 1995;Mé né trey et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Interconversion of Two GDP-Bound Conformations and Their Selection in an Arf-Family Small G Protein

et al. 2011

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ADP-ribosylation factor (Arf) and other Arf-family small G proteins participate in many cellular functions via their characteristic GTP/GDP conformational cycles, during which a nucleotide(∗)Mg(2+)-binding site communicates with a remote N-terminal helix. However, the conformational interplay between the nucleotides, the helix, the protein core, and Mg(2+) has not been fully delineated. Herein, we report a study of the dynamics of an Arf-family protein, Arl8, under various conditions by means of NMR relaxation spectroscopy. The data indicated that, when GDP is bound, the protein core, which does not include the N-terminal helix, reversibly transition between an Arf-family GDP form and another conformation that resembles the Arf-family GTP form. Additionally, we found that the N-terminal helix and Mg(2+), respectively, stabilize the aforementioned former and latter conformations in a population-shift manner. Given the dynamics of the conformational changes, we can describe the Arl8 GTP/GDP cycle in terms of an energy diagram.

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Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion

Boman

Kuai

Zhu

et al. 1999

Cell Motil. Cytoskeleton

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The amino terminus of ADP-ribosylation factor (ARF) 1 is essential for interaction with Gs and ARF GTPase-activating protein.

Cited by 58 publications

References 21 publications

The Myristoylated Amino Terminus of ADP-ribosylation Factor 1 Is a Phospholipid- and GTP-sensitive Switch

The Myristoylated Amino Terminus of ADP-ribosylation Factor 1 Is a Phospholipid- and GTP-sensitive Switch

Interconversion of Two GDP-Bound Conformations and Their Selection in an Arf-Family Small G Protein

Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion

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