The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3

Veltel, Stefan; Gasper, Raphael; Eisenacher, Elke; Wittinghofer, Alfred

doi:10.1038/nsmb.1396

Cited by 162 publications

(221 citation statements)

References 51 publications

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“…Additionally, it was shown that the GDP-form of Arl2 binds the tubulin-specific folding cofactor D (CoD) and that this interaction regulates tubulin folding, microtubule dynamics and the disassembly of the apical junctional complex [6][7][8]. Another tubulin-specific folding cofactor, CoC, is a GTPase-activating protein (GAP) for Arl3 [9]. Arl3 was found in screens for ciliary genes [10,11] and localizes to the connecting cilium of human photoreceptor cells, in line with observations that ciliary proteins are responsible for a range of diseases like polycystic kidney disease or retinitis pigmentosa [12,13].…”

Section: Introductionmentioning

confidence: 99%

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

et al. 2008

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Arl2 and Arl3, members of the Arf subfamily of small G proteins, are believed to be involved in ciliary and microtubuledependent processes. Recently, we could identify RP2, responsible for a variant of X-linked retinitis pigmentosa, as the Arl3-specific GAP. Here, we have characterized Arl2/3 interactions. We show the formation of a ternary complex between Arl3, its cognate GAP RP2 and its retinal effector HRG4. This complex seems to be important for photoreceptor function.

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Section: Introductionmentioning

confidence: 99%

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

et al. 2008

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“…We did not obtain the corresponding reaction intermediates in the Ras-GAP catalyzed GTP hydrolysis; however we could locate such intermediate in simulations of GTP hydrolysis by another GTPase, Arl3, complexed with its GAP, RP2. 43 Even in this case, the next step from this intermediate with the protonated carbonyl oxygen of Gln again resulted in the tautomer imide form of glutamine.…”

Section: New Piecesmentioning

confidence: 99%

Hydrolysis of Guanosine Triphosphate (GTP) by the Ras·GAP Protein Complex: Reaction Mechanism and Kinetic Scheme

et al. 2015

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Molecular mechanisms of hydrolysis of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (Pi) by the Ras·GAP protein complex are fully investigated by using modern modeling tools. The previously hypothesized stages of the cleavage of the phosphorus-oxygen bond in GTP and the formation of the imide form of catalytic Gln61 from Ras upon creation of Pi are confirmed by using the higher-level quantum-based calculations. The steps of the enzyme regeneration are modeled for the first time, providing a comprehensive description of the catalytic cycle. It is found that for the reaction Ras·GAP·GTP·H 2 O → Ras·GAP·GDP·Pi the highest barriers correspond to the process of regeneration of the active site, but not to the process of substrate cleavage. The specific shape of the energy profile is responsible for an interesting kinetic mechanism of the GTP hydrolysis. The analysis of the process using the first-passage approach and consideration of kinetic equations suggest that the overall reactions rate is a result of the balance between relatively fast transitions and low probability of states from which these transitions are taking place. Our theoretical predictions are in excellent agreement with available experimental observations on GTP hydrolysis rates.3

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“…The GAP activity of RP2 and TBCC relies on the TBCC domain and many of the RP2 mutations involved in the retinitis pigmentosa pathology occur in this domain (109). Among the amino acid residues conserved between RP2 and TBCC that are important for their function, it is an arginine residue crucial for their GAP activity, which when mutated provokes retinitis pigmentosa (112). RP2 localizes at the cytoplasm and at the cellular and cilia membranes depending on these localizations on posttranslational modifications such as myristoylation and palmitoylation of its amino terminus (110).…”

Section: The Ciliary Roles Of Tubulin Folding Pathway Members and Relmentioning

confidence: 99%

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

Gonçalves¹,

Tavares²,

Carvalhal³

et al. 2010

BioMolecular Concepts

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Centrosomes and cilia are critical eukaryotic organelles which have been in the spotlight in recent years given their implication in a myriad of cellular and developmental processes. Despite their recognized importance and intense study, there are still many open questions about their biogenesis and function. In the present article, we review the existing data concerning members of the tubulin folding pathway and related proteins, which have been identified at centrosomes and cilia and were shown to have unexpected roles in these structures.

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The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3

Cited by 162 publications

References 51 publications

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex

Hydrolysis of Guanosine Triphosphate (GTP) by the Ras·GAP Protein Complex: Reaction Mechanism and Kinetic Scheme

Revisiting the tubulin folding pathway: new roles in centrosomes and cilia

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