caa a22 4500 606174753 CHVBK 20210128100739.0 cr unu---uuuuu 210128e20150801xx s 000 0 eng 10.1007/s00018-015-1890-6 doi (NATIONALLICENCE)springer-10.1007/s00018-015-1890-6 F -actin binding protein, anillin, regulates integrity of intercellular junctions in human epithelial cells [Elektronische Daten] [Dongdong Wang, Gibran Chadha, Alex Feygin, Andrei Ivanov] Tight junctions (TJ) and adherens junctions (AJ) are key morphological features of differentiated epithelial cells that regulate the integrity and permeability of tissue barriers. Structure and remodeling of epithelial junctions depends on their association with the underlying actomyosin cytoskeleton. Anillin is a unique scaffolding protein interacting with different cytoskeletal components, including actin filaments and myosin motors. Its role in the regulation of mammalian epithelial junctions remains unexplored. Downregulation of anillin expression in human prostate, colonic, and lung epithelial cells triggered AJ and TJ disassembly without altering the expression of junctional proteins. This junctional disassembly was accompanied by dramatic disorganization of the perijunctional actomyosin belt; while the general architecture of the actin cytoskeleton, and activation status of non-muscle myosin II, remained unchanged. Furthermore, loss of anillin disrupted the adducin-spectrin membrane skeleton at the areas of cell-cell contact, selectively decreased γ-adducin expression, and induced cytoplasmic aggregation of αII-spectrin. Anillin knockdown activated c-Jun N-terminal kinase (JNK), and JNK inhibition restored AJ and TJ integrity and cytoskeletal organization in anillin-depleted cells. These findings suggest a novel role for anillin in regulating intercellular adhesion in model human epithelia by mechanisms involving the suppression of JNK activity and controlling the assembly of the perijunctional cytoskeleton. Springer Basel, 2015 Tight junctions nationallicence Adherens junctions nationallicence Non-muscle myosin II nationallicence Adducin nationallicence Spectrin nationallicence JNK nationallicence Wang Dongdong Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut Chadha Gibran Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut Feygin Alex Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut Ivanov Andrei Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut Cellular and Molecular Life Sciences Springer Basel 72/16(2015-08-01), 3185-3200 1420-682X 72:16<3185 2015 72 18 https://doi.org/10.1007/s00018-015-1890-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-1890-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Wang Dongdong Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut NATIONALLICENCE 700 1- Chadha Gibran Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut NATIONALLICENCE 700 1- Feygin Alex Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut NATIONALLICENCE 700 1- Ivanov Andrei Department of Human and Molecular Genetics, Virginia Commonwealth University, 401 College Street, Box 980035, 23298, Richmond, VA, USA aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/16(2015-08-01), 3185-3200 1420-682X 72:16<3185 2015 72 18