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Zhang, X.; Cao, S.; Barila, G.; Edreira, M.M.; Wankhede, M.; Naim, N.; Buck, M.; Altschuler, D.L. "Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase" (2018) Journal of Biological Chemistry. 293(20)
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Abstract:

Rap1 proteins are members of the Ras subfamily of small GTPases involved in many biological responses, including adhesion, cell proliferation, and differentiation. Like all small GTPases, they work as molecular allosteric units that are active in signaling only when associated with the proper membrane compartment. Prenylation, occurring in the cytosol, is an enzymatic posttranslational event that anchors small GTPases at the membrane, and prenyl-binding proteins are needed to mask the cytoplasm-exposed lipid during transit to the target membrane. However, several of these proteins still await discovery. In this study, we report that cyclase-associated protein 1 (CAP1) binds Rap1. We found that this binding is GTP-independent, does not involve Rap1's effector domain, and is fully contained in its C-terminal hypervariable region (HVR). Furthermore, Rap1 prenylation was required for high-affinity interactions with CAP1 in a geranylgeranyl-specific manner. The prenyl binding specifically involved CAP1's C-terminal hydrophobic -sheet domain. We present a combination of experimental and computational approaches, yielding a model whereby the high-affinity binding between Rap1 and CAP1 involves electrostatic and nonpolar side-chain interactions between Rap1's HVR residues, lipid, and CAP1 -sheet domain. The binding was stabilized by the lipid insertion into the -solenoid whose interior was occupied by nonpolar side chains. This model was reminiscent of the recently solved structure of the PDE-K-Ras complex; accordingly, disruptors of this complex, e.g. deltarasin, blocked the Rap1-CAP1 interaction. These findings indicate that CAP1 is a geranylgeranyl-binding partner of Rap1. © 2018 Zhang et al.

Registro:

Documento: Artículo
Título:Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase
Autor:Zhang, X.; Cao, S.; Barila, G.; Edreira, M.M.; Wankhede, M.; Naim, N.; Buck, M.; Altschuler, D.L.
Filiación:Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, United States
Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, OH 44116, United States
Center for Research on Reproduction and Women's Health, University of Pennsylvania Health System, Philadelphia, PA 19104, United States
IQUIBICEN-CONICET, Instituto en el Departamento de Química Biológica de la Facultad de Cíencias Exactas y Naturales, Universídad de Buenos Aires - Consejo Nacional de Investigaciones Cientí-ficas y Técnícas, Ciudad Autónoma de Buenos Aires, C1428EGA, Argentina
Dept. of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, W1346 Biomedical Science Tower, 200 Lothrop St., Pittsburgh, PA 15261, United States
Palabras clave:Cell proliferation; Chains; Cytology; Binding partners; Biological response; Computational approach; Effector domains; High affinity binding; Membrane compartment; Prenyl-binding proteins; Side-chain interactions; Proteins; binding protein; cyclase associated protein 1; lipid; prenylamine; Rap1 protein; unclassified drug; CAP1 protein, human; cell cycle protein; cytoskeleton protein; diterpene; geranylgeranic acid; Rap protein; RAP1B protein, human; animal cell; beta sheet; binding affinity; carboxy terminal sequence; controlled study; human; human cell; nonhuman; priority journal; protein binding; protein domain; protein prenylation; protein protein interaction; rat; Review; static electricity; animal; cell culture; chemistry; genetics; metabolism; molecular dynamics; molecular model; protein conformation; protein prenylation; thyroid follicular cell; Animals; Cell Cycle Proteins; Cells, Cultured; Cytoskeletal Proteins; Diterpenes; Humans; Models, Molecular; Molecular Dynamics Simulation; Protein Conformation; Protein Prenylation; rap GTP-Binding Proteins; Rats; Thyroid Epithelial Cells
Año:2018
Volumen:293
Número:20
DOI: http://dx.doi.org/10.1074/jbc.RA118.001779
Título revista:Journal of Biological Chemistry
Título revista abreviado:J. Biol. Chem.
ISSN:00219258
CODEN:JBCHA
CAS:lipid, 66455-18-3; prenylamine, 390-64-7; CAP1 protein, human; Cell Cycle Proteins; Cytoskeletal Proteins; Diterpenes; geranylgeranic acid; rap GTP-Binding Proteins; RAP1B protein, human
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00219258_v293_n20_p_Zhang

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Citas:

---------- APA ----------
Zhang, X., Cao, S., Barila, G., Edreira, M.M., Wankhede, M., Naim, N., Buck, M.,..., Altschuler, D.L. (2018) . Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase. Journal of Biological Chemistry, 293(20).
http://dx.doi.org/10.1074/jbc.RA118.001779
---------- CHICAGO ----------
Zhang, X., Cao, S., Barila, G., Edreira, M.M., Wankhede, M., Naim, N., et al. "Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase" . Journal of Biological Chemistry 293, no. 20 (2018).
http://dx.doi.org/10.1074/jbc.RA118.001779
---------- MLA ----------
Zhang, X., Cao, S., Barila, G., Edreira, M.M., Wankhede, M., Naim, N., et al. "Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase" . Journal of Biological Chemistry, vol. 293, no. 20, 2018.
http://dx.doi.org/10.1074/jbc.RA118.001779
---------- VANCOUVER ----------
Zhang, X., Cao, S., Barila, G., Edreira, M.M., Wankhede, M., Naim, N., et al. Cyclase-associated protein 1 (CAP1) is a prenyl-binding partner of Rap1 GTPase. J. Biol. Chem. 2018;293(20).
http://dx.doi.org/10.1074/jbc.RA118.001779