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80 results on '"Arendt, Anatol"'

9. Identification of a guanylyl cyclase-activating protein-binding site within the catalytic domain of retinal guanylyl cyclase 1

Author

Sokal, Izabela, Haeseleer, Francoise, Arendt, Anatol, Adman, Elinor T., Hargrave, Paul A., and Palczewski, Krzysztof

Subjects
Cyclic guanylic acid -- Research, Proteins -- Analysis, Catalysis -- Analysis, Binding sites (Biochemistry) -- Research, Biological sciences, Chemistry
Abstract

The intracellular fragment of guanylyl cyclase 1 (GC1), residues 491-1110, were synthesized as a set of 15 amino acids long that partially overlap peptides on the surface of individual pins arranged in a microtiter plate format. This was done to identify regions within photoreceptor GC1 interacting with GC-activating proteins (GCAPs). The results suggested that GC1-GCAP interaction leads to adenylyl cyclase (AC) activation and that the modulation of both GC and AC activity may be done via their own regions in catalytic domains despite interaction with varied activating proteins.

Published
1999

10. Functional reconstitution of photoreceptor guanylate cyclase with native and mutant forms of guanylate cyclase-activating protein 1

Author

Otto-Bruc, Annie, Buczylko, Janina, Surgucheva, Irina, Subbaraya, Iswari, Rudnicka-Nawrot, Maria, Crabb, John W., Arendt, Anatol, Hargrave, Paul A., Baehr, Wolfgang, and Palczewski, Krzysztof

Subjects
Calcium-binding proteins -- Research, Carrier proteins -- Research, Chemical processes -- Research, Photoreceptors -- Research, Proteins -- Research, Biological sciences, Chemistry
Abstract

A study investigated the role of the Ca2+-binding protein in the activation of particulate guanylate cyclase in rod and cone photoreceptor cells using biochemical and biophysical methods. It was found that simulation of particulate guanylate cyclase in rod and cone photoreceptor cells by the Ca2+-binding protein involves several regions of this protein including the N-terminal region. It is proposed that this protein stimulates guanylate cyclase via its intracellular domain in an interaction enhanced by adenosine triphosphate.

Published
1997

17. Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit

Author

Hamm, Heidi E., Deretic, Dusanka, Arendt, Anatol, Hargrave, Paul A., Koenig, Bernd, and Hofmann, Klaus P.

Subjects
Rhodopsin -- Research, Membrane proteins -- Research, Transducin -- Research, Science and technology, Research
Abstract

Site of G Protein Binding to Rhodopsin Mapped with Synthetic Peptides from the α Subunit THE TRANSDUCTION OF BIOLOGICAL signals such as light, hormones, and neurotransmitters starts by a specific [...]

Published
1988

20. Constraints on the conformation of the cytoplasmic face of dark-adapted and light-excited rhodopsin inferred from antirhodopsin antibody imprints

Author

Bailey, Brian W., primary, Mumey, Brendan, additional, Hargrave, Paul A., additional, Arendt, Anatol, additional, Ernst, Oliver P., additional, Hofmann, Klaus Peter, additional, Callis, Patrik R., additional, Burritt, James B., additional, Jesaitis, Algirdas J., additional, and Dratz, Edward A., additional

Published
2009
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24. Identification of regions of arrestin that bind to rhodopsin

Author

Smith, W. Clay, McDowell, J. Hugh, Dugger, Donald R., Miller, Ron, Arendt, Anatol, Popp, Michael P., and Hargrave, Paul A.

Subjects
Rhodopsin -- Analysis, Binding sites (Biochemistry) -- Analysis, Biological sciences, Chemistry
Abstract

Determination of the regions of arrestin binding to rhodopsin was done via binding of random portions of arrestin to R*P and a library of two sets of overlapping synthetic 20-residue peptides that covers arrestin's entire sequence. The results revealed that the synthetic peptide residues 109-130 inhibit the binding of arrestin to rhodopsin with an IC50 of 1.1 mM. Moreover, it was also suggested that a principal binding domain for rhodopsin is contained in the region of residues 101-130 of arrestin.

Published
1999

26. Rhodopsin C-Terminal Sequence Qvs(A)Pa Directs Its Sorting To The Ros In Retinal Photoreceptors.

Author

Hollyfield, Joe G., Anderson, Robert E., LaVail, Matthew M., Deretic, Dusanka, Schmerl, Sonia, Hargrave, Paul A., Arendt, Anatol, and McDowell, J. Hugh

Abstract

Several mutations that cause severe forms of autosomal dominant retinitis pigmentosa (ADRP) cluster in the C-terminal region of rhodopsin. Recent studies have implicated the C-terminal domain of rhodopsin in its trafficking on specialized post-Golgi membranes to the rod outer segment (ROS) of the photoreceptor cell. In addition, aberrant subcellular localization of rhodopsin has been observed in transgenic animals carrying C-terminal mutations. To test if sequence within the C-terminal domain regulates rhodopsin sorting to the ROS, we tested the effects of synthetic peptides that mimic this domain on intracellular trafficking of rhodopsin reconstituted in the frog retinal cell free system. The rhodopsin C-terminal sequence QVS(A)PA is highly conserved among different species. Synthetic peptides corresponding to the C-terminal of frog (AA 330-354) and bovine (AA 324-348) rhodopsin inhibited post-Golgi trafficking by 60% and 50%, respectively, and arrested newly synthesized rhodopsin in the trans-Golgi network (TGN). Peptides corresponding to the cytoplasmic loops and several control peptides had no effect. To assess the role of the last 5 amino acids QVS(A)PA in rhodopsin trafficking, and to model three naturally occurring mutations: Q344ter (lacking the last 5 amino acids QVAPA), V345M and P347S, we introduced equivalent substitutions into the frog C-terminal peptide. Each of these substitutions completely abolished the inhibitory activity of the peptides. Our data could help to explain detrimental effect of mutant rhodopsin in patients with ADRP. We propose that amino acids QVS(A)PA comprise a sorting signal that is recognized by specific factor(s) in the trans-Golgi network. A lack of recognition of this sequence, due to mutations in the last five amino acids causing ADRP most likely results in abnormal post-Golgi membrane formation and in an aberrant subcellular localization of rhodopsin. [ABSTRACT FROM AUTHOR]

Published
1999
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28. Synthesis of Phosphopeptides Containing O-Phosphoserine and O-Phosphothreonine.

Author

Walker, John M., Pennington, Michael W., Dunn, Ben M., Arendt, Anatol, and Hargrave, Paul A.

Abstract

Phosphorylation and dephosphorylation of proteins represents one of the most widespread and important reactions in the regulation of cellular processes. Specific serine, threonine, or tyrosine residues in substrate proteins become phosphorylated by the action of protein kinases that catalyze the transfer of phosphate from high-energy nucleoside triphosphate. Major proteins in bones, teeth, eggs, and milk are highly phosphorylated. Preparation of phosphopeptides related to sequences of phosphoproteins is important for the study of their properties. Enzymatic methods for the synthesis of phosphopeptides can be useful, but are limited to very specific peptide sequences. [ABSTRACT FROM AUTHOR]

Published
1995
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32. Constraints on the conformation of the cytoplasmic face of dark-adapted and light-excited rhodopsin inferred from antirhodopsin antibody imprints.

Author

Bailey, Brian W., Mumey, Brendan, Hargrave, Paul A., Arendt, Anatol, Ernst, Oliver P., Hofmann, Klaus Peter, Callis, Patrik R., Burritt, James B., Jesaitis, Algirdas J., and Dratz, Edward A.

Abstract

Rhodopsin is the best-understood member of the large G protein-coupled receptor (GPCR) superfamily. The G-protein amplification cascade is triggered by poorly understood light-induced conformational changes in rhodopsin that are homologous to changes caused by agonists in other GPCRs. We have applied the 'antibody imprint' method to light-activated rhodopsin in native membranes by using nine monoclonal antibodies (mAbs) against aqueous faces of rhodopsin. Epitopes recognized by these mAbs were found by selection from random peptide libraries displayed on phage. A new computer algorithm, FINDMAP, was used to map the epitopes to discontinuous segments of rhodopsin that are distant in the primary sequence but are in close spatial proximity in the structure. The proximity of a segment of the N-terminal and the loop between helices VI and VIII found by FINDMAP is consistent with the X-ray structure of the dark-adapted rhodopsin. Epitopes to the cytoplasmic face segregated into two classes with different predicted spatial proximities of protein segments that correlate with different preferences of the antibodies for stabilizing the metarhodopsin I or metarhodopsin II conformations of light-excited rhodopsin. Epitopes of antibodies that stabilize metarhodopsin II indicate conformational changes from dark-adapted rhodopsin, including rearrangements of the C-terminal tail and altered exposure of the cytoplasmic end of helix VI, a portion of the C-3 loop, and helix VIII. As additional antibodies are subjected to antibody imprinting, this approach should provide increasingly detailed information on the conformation of light-excited rhodopsin and be applicable to structural studies of other challenging protein targets. [ABSTRACT FROM AUTHOR]

Published
2003
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