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Your search keyword '"Soss, Sarah E."' showing total 19 results
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19 results on '"Soss, Sarah E."'

1. Functional implications for a prototypical K-turn binding protein from structural and dynamical studies of 15.5K

Author

Soss, Sarah E. and Flynn, Peter F.

Subjects
Binding proteins -- Research, Binding proteins -- Chemical properties, Nuclear magnetic resonance spectroscopy -- Usage, Biological sciences, Chemistry
Abstract

A solution NMR-based studies which provide insight into the structure, function, and dynamics of 15.5K in the Kink-turn protein-RNA interaction is described.

Published
2007

3. Disrupted structure and aberrant function of CHIP mediates the loss of motor and cognitive function in preclinical models of SCAR16

Author

Shi, Chang-he, primary, Rubel, Carrie, additional, Soss, Sarah E., additional, Sanchez-Hodge, Rebekah, additional, Zhang, Shuo, additional, Madrigal, Sabrina C., additional, Ravi, Saranya, additional, McDonough, Holly, additional, Page, Richard C., additional, Chazin, Walter J., additional, Patterson, Cam, additional, Mao, Cheng-yuan, additional, Willis, Monte S., additional, Luo, Hai-Yang, additional, Li, Yu-sheng, additional, Stevens, Donte A., additional, Tang, Mi-bo, additional, Du, Pan, additional, Wang, Yao-he, additional, Hu, Zheng-wei, additional, Xu, Yu-ming, additional, and Schisler, Jonathan C., additional

Published
2018
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4. Disrupted structure and aberrant function of CHIP mediates the loss of motor and cognitive function in preclinical models of cerebellar CHIPopathy

Author

Shi, Chang-he, primary, Rubel, Carrie, additional, Soss, Sarah E., additional, Sanchez-Hodge, Rebekah, additional, Zhang, Shuo, additional, Stevens, Donte A., additional, McDonough, Holly, additional, Page, Richard C., additional, Chazin, Walter J., additional, Patterson, Cam, additional, Mao, Cheng-yuan, additional, Willis, Monte S., additional, Luo, Hai-Yang, additional, Tang, Mi-bo, additional, Du, Pan, additional, Wang, Yao-he, additional, Hu, Zheng-wei, additional, Xu, Yu-ming, additional, and Schisler, Jonathan C., additional

Published
2018
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5. Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination

Author

McConnell, Jamie L., Watkins, Guy R., Soss, Sarah E., Franz, Heidi S., McCorvey, Lisa R., Spiller, Benjamin W., Chazin, Walter J., and Wadzinski, Brian E.

Subjects
Catalysis -- Analysis, Protein binding -- Analysis, Serine -- Chemical properties, Serine -- Structure, Threonine -- Chemical properties, Threonine -- Structure, Ubiquitin -- Chemical properties, Ubiquitin -- Structure, Biological sciences, Chemistry
Abstract

The significant role of alpha4 which is a PP2Ac-interacting adaptor protein that provides a binding platform for both protein serine/threonine phosphatase 2A catalytic subunit (PP2Ac) and ubiquitin ligase Mid1 is described. The results offer insight into the polyubiquitination of PP2Ac which is inhibited by the UIM within alpha4 and the direct regulation of PP2Ac polyubiquitination by a novel UIM within the adaptor protein alpha4.

Published
2010

6. Structural and functional characterization of the monomeric U-box domain from E4

Author

Nordquist, Kyle A., Dimitrova, Yoana N., Brzovic, Peter S., Ridenour, Whitney B., Munro, Kim A., Soss, Sarah E., Caprioli, Richard M., Klevit, Rachel E., and Chazin, Walter J.

Subjects
Ligases -- Chemical properties, Ligases -- Structure, Nuclear magnetic resonance spectroscopy -- Usage, Protein folding -- Analysis, Ubiquitin-proteasome system -- Analysis, Biological sciences, Chemistry
Abstract

The structural and functional characterization of the yeast U-box protein Ufd2 and its mammalian homologue E4B is reported. E4BU is a stable monomeric protein that folds into the same structure observed for other structurally characterized U-box domain homodimers.

Published
2010

8. Activation of UbcH5c∼Ub Is the Result of a Shift in Interdomain Motions of the Conjugate Bound to U-Box E3 Ligase E4B

Author

Soss, Sarah E., Klevit, Rachel E., and Chazin, Walter J.

Abstract

Post-translational modification of proteins with ubiquitin is mediated by dynamic multienzyme machinery (E1, E2, and E3). E3 ubiquitin ligases play a key role acting as both scaffolds to bring reactants together and activators to catalyze ubiquitin (Ub) transfer from E2∼Ub conjugates to substrates. Our recent studies provided insights into the mechanism of the activation event; binding of an E3 to an E2∼Ub conjugate was found to affect the motions of E2∼Ub and allosterically stimulate Ub transfer. This proposed mechanism implies that the dynamics of the conjugate, which has been shown to occupy a wide range of E2∼Ub orientations, will be altered significantly upon binding of E3. To directly assess the effect of E3 binding on E2∼Ub dynamics, we undertook an in-depth comparative analysis of 15N nuclear magnetic resonance relaxation of UbcH5c∼Ub in the absence and presence of the E3 ligase, E4B. Challenges encountered in deciphering interdomain motions for this ternary complex are discussed along with the limitations of the current approaches. Notably, although a reduction in interdomain dynamics of UbcH5c∼Ub is observed upon binding to E4B, Ub retains an extensive degree of flexibility. These results provide strong support for our dynamic model of a significant orientational bias of Ub toward a more closed conformation in the E3/E2∼Ub complex.

Published
2024
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