TY - CHAP AU - Migh, Ede AU - Földi, István AU - Molnár, Imre Árpád AU - Szikora, Szilárd ED - Vágvölgyi, Csaba ED - Siklós, László TI - Developmental signaling pathways in human cancer T2 - Selected Topics from Contemporary Experimental Biology, Volume 2 PB - MTA Szegedi Biológiai Központ CY - Szeged PY - 2015 SP - 171 EP - 188 PG - 18 UR - https://m2.mtmt.hu/api/publication/3003062 ID - 3003062 LA - English DB - MTMT ER - TY - THES AU - Molnár, Imre Árpád TI - A DAAM formin alcsalád szerepe az izomfejlődésben PB - Szegedi Tudományegyetem (SZTE) PY - 2015 SP - 115 DO - 10.14232/phd.2422 UR - https://m2.mtmt.hu/api/publication/2756659 ID - 2756659 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Molnár, Imre Árpád AU - Migh, Ede AU - Szikora, Szilárd AU - Kalmár, Tibor AU - Végh, Attila Gergely AU - Deák, Ferenc AU - Barkó, Szilvia AU - Bugyi, Beáta AU - Orfanos, Zacharias AU - Kovács, János AU - Juhász, Gábor AU - Váró, György AU - Nyitrai, Miklós AU - Sparrow, John AU - Mihály, József TI - DAAM is required for thin filament formation and sarcomerogenesis during muscle development in Drosophila JF - PLOS GENETICS J2 - PLOS GENET VL - 10 PY - 2014 IS - 2 PG - 15 SN - 1553-7390 DO - 10.1371/journal.pgen.1004166 UR - https://m2.mtmt.hu/api/publication/2506301 ID - 2506301 AB - During muscle development, myosin and actin containing filaments assemble into the highly organized sarcomeric structure critical for muscle function. Although sarcomerogenesis clearly involves the de novo formation of actin filaments, this process remained poorly understood. Here we show that mouse and Drosophila members of the DAAM formin family are sarcomere-associated actin assembly factors enriched at the Z-disc and M-band. Analysis of dDAAM mutants revealed a pivotal role in myofibrillogenesis of larval somatic muscles, indirect flight muscles and the heart. We found that loss of dDAAM function results in multiple defects in sarcomere development including thin and thick filament disorganization, Z-disc and M-band formation, and a near complete absence of the myofibrillar lattice. Collectively, our data suggest that dDAAM is required for the initial assembly of thin filaments, and subsequently it promotes filament elongation by assembling short actin polymers that anneal to the pointed end of the growing filaments, and by antagonizing the capping protein Tropomodulin. LA - English DB - MTMT ER - TY - JOUR AU - Nelson, KS AU - Khan, Z AU - Molnár, Imre Árpád AU - Mihály, József AU - Kaschube, M AU - Beitel, GJ TI - Drosophila Src regulates anisotropic apical surface growth to control epithelial tube size JF - NATURE CELL BIOLOGY J2 - NAT CELL BIOL VL - 14 PY - 2012 IS - 5 SP - 518 EP - 525 PG - 8 SN - 1465-7392 DO - 10.1038/ncb2467 UR - https://m2.mtmt.hu/api/publication/2015355 ID - 2015355 AB - Networks of epithelial and endothelial tubes are essential for the function of organs such as the lung, kidney and vascular system. The sizes and shapes of these tubes are highly regulated to match their individual functions. Defects in tube size can cause debilitating diseases such as polycystic kidney disease and ischaemia(1,2). It is therefore critical to understand how tube dimensions are regulated. Here we identify the tyrosine kinase Src as an instructive regulator of epithelial-tube length in the Drosophila tracheal system. Loss-of-function Src42 mutations shorten tracheal tubes, whereas Src42 overexpression elongates them. Surprisingly, Src42 acts distinctly from known tube-size pathways and regulates both the amount of apical surface growth and, with the conserved formin dDaam, the direction of growth. Quantitative three-dimensional image analysis reveals that Src42- and dDaam-mutant tracheal cells expand more in the circumferential than the axial dimension, resulting in tubes that are shorter in length-but larger in diameter-than wild-type tubes. Thus, Src42 and dDaam control tube dimensions by regulating the direction of anisotropic growth, a mechanism that has not previously been described. LA - English DB - MTMT ER - TY - JOUR AU - Prokop, A AU - Sanchez-Soriano, N AU - Goncalves-Pimentel, C AU - Molnár, Imre Árpád AU - Kalmár, Tibor AU - Mihály, József TI - DAAM family members leading a novel path into formin research. JF - COMMUNICATIVE AND INTEGRATIVE BIOLOGY J2 - COMMUN INTEGR BIOL VL - 4 PY - 2011 IS - 5 SP - 538 EP - 542 PG - 5 SN - 1942-0889 DO - 10.4161/cib.16511 UR - https://m2.mtmt.hu/api/publication/1921932 ID - 1921932 AB - Formins are an important and evolutionarily well conserved class of actin binding proteins with essential biological functions. Although their molecular roles in actin regulation have been clearly demonstrated in vitro, their functions at the cellular or organism levels are still poorly understood. To illustrate this problem, but also to demonstrate potential ways forward, we focus here on the DAAM group of formins. In vertebrates, DAAM group members have been demonstrated to be important regulators of cellular and tissue morphogenesis but, as for all formins, the molecular mechanisms underlying these morphogenetic functions remain to be uncovered. The genome of the fruitfly Drosophila encodes a single DAAM gene that is evolutionarily highly conserved. Recent work on dDAAM has already provided a unique combination of observations and experimental opportunities unrivalled by any other Drosophila formin. These comprise in vitro actin polymerisation assays, subcellular studies in culture and in vivo, and a range of developmental phenotypes revealing a role in tracheal morphogenesis, axonal growth and muscle organization. At all these levels, future work on dDAAM will capitalize on the power of fly genetics, raising unique opportunities to advance our understanding of dDAAM at the systems level, with obvious implications for other formins. LA - English DB - MTMT ER -