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20 results on '"Cubuk, Jasmine"'

6. Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms

Author

Stuchell-Brereton, Melissa D., primary, Zimmerman, Maxwell I., additional, Miller, Justin J., additional, Mallimadugula, Upasana L., additional, Incicco, J. Jeremías, additional, Roy, Debjit, additional, Smith, Louis G., additional, Cubuk, Jasmine, additional, Baban, Berevan, additional, DeKoster, Gregory T., additional, Frieden, Carl, additional, Bowman, Gregory R., additional, and Soranno, Andrea, additional

Published
2023
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7. Single-molecule spectroscopy of Apolipoprotein E reveals a complex conformational ensemble

Author

Stuchell-Brereton, Melissa D., primary, Zimmerman, Maxwell I., additional, Miller, Justin J., additional, Mallimadugula, Upasana L., additional, Incicco, Juan J., additional, Roy, Debjit, additional, Smith, Louis G., additional, Cubuk, Jasmine, additional, Baban, Berevan, additional, DeKoster, Gregory T., additional, Frieden, Carl, additional, Bowman, Gregory R., additional, and Soranno, Andrea, additional

Published
2023
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15. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA

Author

Cubuk, Jasmine, primary, Alston, Jhullian J., additional, Incicco, J. Jeremías, additional, Singh, Sukrit, additional, Stuchell-Brereton, Melissa D., additional, Ward, Michael D., additional, Zimmerman, Maxwell I., additional, Vithani, Neha, additional, Griffith, Daniel, additional, Wagoner, Jason A., additional, Bowman, Gregory R., additional, Hall, Kathleen B., additional, Soranno, Andrea, additional, and Holehouse, Alex S., additional

Published
2020
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19. Structural dynamics of the intrinsically disordered linker region of cardiac troponin T.

Author

Cubuk J, Greenberg L, Greenberg AE, Emenecker RJ, Stuchell-Brereton MD, Holehouse AS, Soranno A, and Greenberg MJ

Abstract

The cardiac troponin complex, composed of troponins I, T, and C, plays a central role in regulating the calcium-dependent interactions between myosin and the thin filament. Mutations in troponin can cause cardiomyopathies; however, it is still a major challenge for the field to connect how changes in sequence affect troponin's function. Recent high-resolution structures of the thin filament revealed critical insights into the structure-function relationship of the troponin complex, but there remain large, unresolved segments of troponin, including the troponin-T linker region that is a hotspot for several cardiomyopathy mutations. This unresolved yet functionally-significant linker region has been proposed to be intrinsically disordered, with behaviors that are not well described by traditional structural approaches; however, this proposal has not been experimentally verified. Here, we used a combination of single-molecule Förster resonance energy transfer (FRET), molecular dynamics simulations, and functional reconstitution assays to investigate the troponin-T linker region. We experimentally and computationally show that in the context of both isolated troponin and the fully regulated troponin complex, the linker behaves as a dynamic, intrinsically disordered region. This region undergoes polyampholyte expansion in the presence of high salt and distinct conformational changes during the assembly of the troponin complex. We also examine the ΔE160 hypertrophic cardiomyopathy mutation in the linker, and we demonstrate that this mutation does not affect the conformational dynamics of the linker, rather it allosterically affects interactions with other subunits of the troponin complex, leading to increased molecular contractility. Taken together, our data clearly demonstrate the importance of disorder within the troponin-T linker and provide new insights into the molecular mechanisms controlling the pathogenesis of cardiomyopathies., Competing Interests: All experiments were conducted in the absence of any commercial or financial relationships that could be construed as potential conflicts of interest.

Published
2024
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20. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA.

Author

Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, and Holehouse AS

Abstract

The SARS-CoV-2 nucleocapsid (N) protein is an abundant RNA binding protein critical for viral genome packaging, yet the molecular details that underlie this process are poorly understood. Here we combine single-molecule spectroscopy with all-atom simulations to uncover the molecular details that contribute to N protein function. N protein contains three dynamic disordered regions that house putative transiently-helical binding motifs. The two folded domains interact minimally such that full-length N protein is a flexible and multivalent RNA binding protein. N protein also undergoes liquid-liquid phase separation when mixed with RNA, and polymer theory predicts that the same multivalent interactions that drive phase separation also engender RNA compaction. We offer a simple symmetry-breaking model that provides a plausible route through which single-genome condensation preferentially occurs over phase separation, suggesting that phase separation offers a convenient macroscopic readout of a key nanoscopic interaction.

Published
2020
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