title: SLK/LOSK kinase regulates cell motility independently of microtubule organization and Golgi polarization.
abstract: Cell motility is an essential complex process that requires actin and microtubule cytoskeleton reorganization and polarization. Such extensive rearrangement is closely related to cell polarization as a whole. The serine/threonine kinase SLK/LOSK is a potential regulator of cell motility, as it phosphorylates a series of cytoskeleton-bound proteins that collectively participate in the remodeling of migratory cell architecture. In this work, we report that SLK/LOSK is an indispensable regulator of cell locomotion that primarily acts through the small GTPase RhoA and the dynactin subunit p150(Glued). Both RhoA and dynactin affect cytoskeleton organization, polarization, and general cell locomotory activity to various extents. However, it seems that these events are independent of each other. Thus, SLK/LOSK kinase effectively functions as a switch that links all of the processes underlying cell motility to provide robust directional movement.
authors.affiliation: A.N.Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskye Gory, Moscow, 119992, Russia.
authors.forename: Artem I
authors.initials: AI
authors.lastname: Fokin
authors.affiliation: Institute of Protein Research of Russian Academy of Sciences, Moscow Region, Pushchino, Institutskaya Str, 4, 142290, Russia.
authors.forename: Tatiana S
authors.initials: TS
authors.lastname: Klementeva
authors.affiliation: A.N.Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskye Gory, Moscow, 119992, Russia.|Institute of Protein Research of Russian Academy of Sciences, Moscow Region, Pushchino, Institutskaya Str, 4, 142290, Russia.
authors.forename: Elena S
authors.initials: ES
authors.lastname: Nadezhdina
authors.affiliation: A.N.Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskye Gory, Moscow, 119992, Russia.
authors.forename: Anton V
authors.initials: AV
authors.lastname: Burakov
mesh_terms: D000818:Animals; D002465:Cell Movement / Q000187:drug effects; D002522:Chlorocebus aethiops; D006056:Golgi Apparatus / Q000187:drug effects / Q000378:metabolism*; D057809:HEK293 Cells; D006801:Humans; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism*; D008954:Models, Biological; D050505:Mutant Proteins / Q000378:metabolism; D047428:Protein Kinase Inhibitors / Q000494:pharmacology; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D013379:Substrate Specificity / Q000187:drug effects; D014709:Vero Cells; D054460:rho-Associated Kinases / Q000378:metabolism; D020742:rhoA GTP-Binding Protein / Q000378:metabolism
chemical_list: D050505:Mutant Proteins; D047428:Protein Kinase Inhibitors; D017346:Protein Serine-Threonine Kinases; D054460:rho-Associated Kinases; D020742:rhoA GTP-Binding Protein
keywords: RhoA; SLK/LOSK; cell motility; dynactin; microtubules