Biophysical Characterization of the Binding Mechanism between the MATH Domain of SPOP and Its Physiological Partners

被引：5

作者：

Diop, Awa ^{[1
]}

Pietrangeli, Paola ^{[1
]}

Nardella, Caterina ^{[1
]}

Pennacchietti, Valeria ^{[1
]}

Pagano, Livia ^{[1
]}

Toto, Angelo ^{[1
]}

Di Felice, Mariana ^{[1
]}

Di Matteo, Sara ^{[1
]}

Marcocci, Lucia ^{[1
]}

Malagrino, Francesca ^{[1
]}

Gianni, Stefano ^{[1
]}

机构：

[1] Sapienza Univ Roma, Fdn Cenci Bolognetti, Ist Pasteur Italia, Dipartimento Sci Biochim A Rossi Fanelli, Ple Aldo Moro 5, I-00185 Rome, Italy

来源：

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2023年 / 24卷 / 12期

关键词：

kinetics; protein-protein interactions; MATH domain; speckle-type POZ protein; PROTEIN;

D O I：

10.3390/ijms241210138

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

SPOP (Speckle-type POZ protein) is an E3 ubiquitin ligase adaptor protein that mediates the ubiquitination of several substrates. Furthermore, SPOP is responsible for the regulation of both degradable and nondegradable polyubiquitination of a number of substrates with diverse biological functions. The recognition of SPOP and its physiological partners is mediated by two protein-protein interaction domains. Among them, the MATH domain recognizes different substrates, and it is critical for orchestrating diverse cellular pathways, being mutated in several human diseases. Despite its importance, the mechanism by which the MATH domain recognizes its physiological partners has escaped a detailed experimental characterization. In this work, we present a characterization of the binding mechanism of the MATH domain of SPOP with three peptides mimicking the phosphatase Puc, the chromatin component MacroH2A, and the dual-specificity phosphatase PTEN. Furthermore, by taking advantage of site-directed mutagenesis, we address the role of some key residues of MATH in the binding process. Our findings are briefly discussed in the context of previously existing data on the MATH domain.

引用

页数：12

共 24 条

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