Crystallization and preliminary X‐ray analysis of arrestin from bovine rod outer segment

Wilden, Ursula; Choe, Huhn; Krafft, Bianca; Granzin, Joachim

doi:10.1016/s0014-5793(97)01137-x

Cited by 6 publications

(2 citation statements)

References 31 publications

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“…The crystal structures of Arrestin family members, including Arr1, Arr4 and β-arrestin1, are remarkably similar (Wilden et al, 1997;Hirsch et al, 1999;Han et al, 2001;Sutton et al, 2005). In a previous in vitro yeast two-hybrid study, β-arrestin1 was shown to interact in vitro with NSF and it bound to the identical region (AA 197-250 of NSF) as observed for Arr1 binding.…”

Section: Discussionmentioning

confidence: 99%

Visual Arrestin 1 Acts As a Modulator for N-Ethylmaleimide-Sensitive Factor in the Photoreceptor Synapse

Huang¹,

Brown²,

Craft³

2010

Journal of Neuroscience

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In the G-protein-coupled receptor phototransduction cascade, visual Arrestin 1 (Arr1) binds to and deactivates phosphorylated light-activated opsins, a process that is critical for effective recovery and normal vision. In this report, we discovered a novel synaptic interaction between Arr1 and N-ethylmaleimide-sensitive factor (NSF) that is enhanced in a dark environment when mouse photoreceptors are depolarized and the rate of exocytosis is elevated. In the photoreceptor synapse, NSF functions to sustain a higher rate of exocytosis, in addition to the compensatory endocytosis to retrieve and to recycle vesicle membrane and synaptic proteins. Not only does Arr1 bind to the junction of NSF N-terminal and its first ATPase domains in an ATP-dependent manner in vitro, but Arr1 also enhances both NSF ATPase and NSF disassembly activities. In in vivo experiments in mouse retinas with the Arr1 gene knocked out, the expression levels of NSF and other synapse-enriched components, including vGLUT1 (vesicular glutamate transporter 1), EAAT5 (excitatory amino acid transporter 5), and VAMP2 (vesicle-associated membrane protein 2), are markedly reduced, which leads to a substantial decrease in the exocytosis rate with FM1-43. Thus, we propose that the Arr1 and NSF interaction is important for modulating normal synaptic function in mouse photoreceptors. This study demonstrates a vital alternative function for Arr1 in the photoreceptor synapse and provides key insights into the potential molecular mechanisms of inherited retinal diseases, such as Oguchi disease and Arr1-associated retinitis pigmentosa.

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Section: Discussionmentioning

confidence: 99%

Visual Arrestin 1 Acts As a Modulator for N-Ethylmaleimide-Sensitive Factor in the Photoreceptor Synapse

Huang¹,

Brown²,

Craft³

2010

Journal of Neuroscience

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“…HiTrap Heparin column and eluted with a 0-1 M NaCl gradient in Buffer A. Arrestin eluted at a concentration of 300 to 400 mM NaCl was dialysed thoroughly against 100 mM NaCl in Buffer A. Purified arrestin was concentrated to 20 mg/ml using Amicon filters (30 kDa cutoff). For crystallization, concentrated arrestin (2 ml) was mixed with reservoir solution (2 ml) consisting of crystallization buffer as described previously (Wilden et al, 1997). Arrestin crystals grew within a week using the hanging-drop method.…”

Section: Tyrosine Fluorescence Quenching Assay Of Arr1mentioning

confidence: 99%