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Systematic identification of recognition motifs for the hub protein LC8
Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA.
Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA.
Oregon State Univ, Dept Biochem & Biophys, Corvallis, OR 97331 USA.ORCID-id: 0000-0003-0533-9225
Univ Coll Dublin, Conway Inst Biomol & Biomed Sci, Dublin, Ireland.
Vise andre og tillknytning
2019 (engelsk)Inngår i: LIFE SCIENCE ALLIANCE, ISSN 2575-1077, Vol. 2, nr 4, artikkel-id e201900366Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Hub proteins participate in cellular regulation by dynamic binding of multiple proteins within interaction networks. The hub protein LC8 reversibly interacts with more than 100 partners through a flexible pocket at its dimer interface. To explore the diversity of the LC8 partner pool, we screened for LC8 binding partners using a proteomic phage display library composed of peptides from the human proteome, which had no bias toward a known LC8 motif. Of the identified hits, we validated binding of 29 peptides using isothermal titration calorimetry. Of the 29 peptides, 19 were entirely novel, and all had the canonical TQT motif anchor. A striking observation is that numerous peptides containing the TQT anchor do not bind LC8, indicating that residues outside of the anchor facilitate LC8 interactions. Using both LC8-binding and nonbinding peptides containing the motif anchor, we developed the "LC8Pred" algorithm that identifies critical residues flanking the anchor and parses random sequences to predict LC8-binding motifs with similar to 78% accuracy. Our findings significantly expand the scope of the LC8 hub interactome.

sted, utgiver, år, opplag, sider
2019. Vol. 2, nr 4, artikkel-id e201900366
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Identifikatorer
URN: urn:nbn:se:uu:diva-396555DOI: 10.26508/lsa.201900366ISI: 000484355500016PubMedID: 31266884OAI: oai:DiVA.org:uu-396555DiVA, id: diva2:1368533
Forskningsfinansiär
Swedish Research Council, C0509201Tilgjengelig fra: 2019-11-07 Laget: 2019-11-07 Sist oppdatert: 2019-11-07bibliografisk kontrollert

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