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In cells, weak and transient protein-protein interactions play critical roles in fine-tuning diverse biological processes. These interactions are commonly mediated by small, compact functional modules, called short linear motifs (SLiMs). Due to their small size and highly flexible nature, SLiMs can carry out diverse molecular functions and can be involved in targeting proteins to specific subcellular locations, regulating the activity and interactions of proteins and aiding the assembly of macromolecular complexes. However, their specific properties also make the 644 TEMATIKUS ÖSSZEÁLLÍTÁS • SZERTEÁGAZÓ BIOINFORMATIKA MAGYARORSZÁGON Magyar Tudomány 179(2018)5 experimental discovery of SLiMs challenging. As a result, SLiM mediated interactions are still largely unexplored. In order to discover novel linear motif classes and their interactions, new bioinformatic approaches are needed. In this work, we introduce a novel bioinformatic method that enables the effective prediction of undiscovered binding partners for a given SLiM-binding domain. The approach was applied to the dynein light chain LC8, that already has several known binding partners but its actual function is still unclear. Our work not only presented novel LC8 binding partners, but also highlighted a new function of LC8 in the regulation of a highly important signaling pathway controlling organ size. Kulcsszavak: bioinformatika, fehérje-fehérje kölcsönhatás, jelátvitel, rendezetlen fehérjék, li-

Új lineáris motívumok azonosítása bioinformatikai módszerekkel az LC8 fehérje kölcsönhatási hálózatában