title: The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactions.
abstract: The STIL protein participates in mitosis and malignant transformation by regulating centrosomal duplication. Using biophysical methods we studied the structure and interactions of STIL. We revealed that its central domain is intrinsically disordered and mediates protein-protein interactions of STIL. The intrinsic disorder may provide STIL with the conformational flexibility required for its multitude binding.
authors.affiliation: Institute of Chemistry, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, Jerusalem 91904, Israel. assaf.friedler@mail.huji.ac.il.
authors.forename: Hadar
authors.initials: H
authors.lastname: Amartely
authors.forename: Ahuvit
authors.initials: A
authors.lastname: David
authors.forename: Mario
authors.initials: M
authors.lastname: Lebendiker
authors.forename: Hadar
authors.initials: H
authors.lastname: Benyamini
authors.forename: Shai
authors.initials: S
authors.lastname: Izraeli
authors.forename: Assaf
authors.initials: A
authors.lastname: Friedler
mesh_terms: D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism*; D002942:Circular Dichroism; D005454:Fluorescence Polarization; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry* / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000737:chemistry* / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D000075223:Poly-ADP-Ribose Binding Proteins; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D044767:Ubiquitin-Protein Ligases
chemical_list: D018797:Cell Cycle Proteins; D047908:Intracellular Signaling Peptides and Proteins; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D000075223:Poly-ADP-Ribose Binding Proteins; C071236:STIL protein, human; C412002:CHFR protein, human; D044767:Ubiquitin-Protein Ligases