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  • Title: An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase.
    Author: Conicella AE, Huang R, Ripstein ZA, Nguyen A, Wang E, Löhr T, Schuck P, Vendruscolo M, Rubinstein JL, Kay LE.
    Journal: Proc Natl Acad Sci U S A; 2020 Oct 20; 117(42):26226-26236. PubMed ID: 33028677.
    Abstract:
    VCP/p97, an enzyme critical to proteostasis, is regulated through interactions with protein adaptors targeting it to specific cellular tasks. One such adaptor, p47, forms a complex with p97 to direct lipid membrane remodeling. Here, we use NMR and other biophysical methods to study the structural dynamics of p47 and p47-p97 complexes. Disordered regions in p47 are shown to be critical in directing intra-p47 and p47-p97 interactions via a pair of previously unidentified linear motifs. One of these, an SHP domain, regulates p47 binding to p97 in a manner that depends on the nucleotide state of p97. NMR and electron cryomicroscopy data have been used as restraints in molecular dynamics trajectories to develop structural ensembles for p47-p97 complexes in adenosine diphosphate (ADP)- and adenosine triphosphate (ATP)-bound conformations, highlighting differences in interactions in the two states. Our study establishes the importance of intrinsically disordered regions in p47 for the formation of functional p47-p97 complexes.
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