@article{MTMT:2931297,
	title = {The Formin DAAM Functions as Molecular Effector of the Planar Cell Polarity Pathway during Axonal Development in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/2931297},
	author = {Gombos, Rita I and Migh, Ede and Antal, Otilia Tamara and Mukherjee, A and Jenny, A and Mihály, József},
	doi = {10.1523/JNEUROSCI.3708-14.2015},
	journal-iso = {J NEUROSCI},
	journal = {JOURNAL OF NEUROSCIENCE},
	volume = {35},
	unique-id = {2931297},
	issn = {0270-6474},
	abstract = {Recent studies established that the planar cell polarity (PCP) pathway is critical for various aspects of nervous system development and function, including axonal guidance. Although it seems clear that PCP signaling regulates actin dynamics, the mechanisms through which this occurs remain elusive. Here, we establish a functional link between the PCP system and one specific actin regulator, the formin DAAM, which has previously been shown to be required for embryonic axonal morphogenesis and filopodia formation in the growth cone. We show that dDAAM also plays a pivotal role during axonal growth and guidance in the adult Drosophila mushroom body, a brain center for learning and memory. By using a combination of genetic and biochemical assays, we demonstrate that Wnt5 and the PCP signaling proteins Frizzled, Strabismus, and Dishevelled act in concert with the small GTPase Rac1 to activate the actin assembly functions of dDAAM essential for correct targeting of mushroom body axons. Collectively, these data suggest that dDAAM is used as a major molecular effector of the PCP guidance pathway. By uncovering a signaling system from the Wnt5 guidance cue to an actin assembly factor, we propose that the Wnt5/PCP navigation system is linked by dDAAM to the regulation of the growth cone actin cytoskeleton, and thereby growth cone behavior, in a direct way.},
	year = {2015},
	eissn = {1529-2401},
	pages = {10154-10167},
	orcid-numbers = {Antal, Otilia Tamara/0000-0001-8321-5039}
}

@article{MTMT:2506301,
	title = {DAAM is required for thin filament formation and sarcomerogenesis during muscle development in Drosophila},
	url = {https://m2.mtmt.hu/api/publication/2506301},
	author = {Molnár, Imre Árpád and Migh, Ede and Szikora, Szilárd and Kalmár, Tibor and Végh, Attila Gergely and Deák, Ferenc and Barkó, Szilvia and Bugyi, Beáta and Orfanos, Zacharias and Kovács, János and Juhász, Gábor and Váró, György and Nyitrai, Miklós and Sparrow, John and Mihály, József},
	doi = {10.1371/journal.pgen.1004166},
	journal-iso = {PLOS GENET},
	journal = {PLOS GENETICS},
	volume = {10},
	unique-id = {2506301},
	issn = {1553-7390},
	abstract = {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.},
	year = {2014},
	eissn = {1553-7404},
	orcid-numbers = {Kalmár, Tibor/0000-0002-0419-2009; Végh, Attila Gergely/0000-0003-0524-0946; Juhász, Gábor/0000-0001-8548-8874; Nyitrai, Miklós/0000-0002-6229-4337}
}

@article{MTMT:2588376,
	title = {Elements of image processing in localization microscopy},
	url = {https://m2.mtmt.hu/api/publication/2588376},
	author = {Rees, EJ and Erdélyi, Miklós and Schierle, GSK and Knight, A and Kaminski, CF},
	doi = {10.1088/2040-8978/15/9/094012},
	journal-iso = {J OPTICS-UK},
	journal = {JOURNAL OF OPTICS},
	volume = {15},
	unique-id = {2588376},
	issn = {2040-8978},
	year = {2013},
	eissn = {2040-8986},
	orcid-numbers = {Erdélyi, Miklós/0000-0002-9501-5752}
}

@article{MTMT:1343165,
	title = {Characterization of the biochemical properties and biological function of the formin homology domains of Drosophila DAAM.},
	url = {https://m2.mtmt.hu/api/publication/1343165},
	author = {Barkó, Szilvia and Bugyi, Beáta and Carlier, MF and Gombos, Rita I and Matusek, Tamás and Mihály, József and Nyitrai, Miklós},
	doi = {10.1074/jbc.M109.093914},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {285},
	unique-id = {1343165},
	issn = {0021-9258},
	abstract = {We characterized the properties of Drosophila melanogaster DAAM-FH2 and DAAM-FH1-FH2 fragments and their interactions with actin and profilin by using various biophysical methods and in vivo experiments. The results show that although the DAAM-FH2 fragment does not have any conspicuous effect on actin assembly in vivo, in cells expressing the DAAM-FH1-FH2 fragment, a profilin-dependent increase in the formation of actin structures is observed. The trachea-specific expression of DAAM-FH1-FH2 also induces phenotypic effects, leading to the collapse of the tracheal tube and lethality in the larval stages. In vitro, both DAAM fragments catalyze actin nucleation but severely decrease both the elongation and depolymerization rate of the filaments. Profilin acts as a molecular switch in DAAM function. DAAM-FH1-FH2, remaining bound to barbed ends, drives processive assembly of profilin-actin, whereas DAAM-FH2 forms an abortive complex with barbed ends that does not support profilin-actin assembly. Both DAAM fragments also bind to the sides of the actin filaments and induce actin bundling. These observations show that the D. melanogaster DAAM formin represents an extreme class of barbed end regulators gated by profilin.},
	year = {2010},
	eissn = {1083-351X},
	pages = {13154-13169},
	orcid-numbers = {Nyitrai, Miklós/0000-0002-6229-4337}
}

@article{MTMT:1914506,
	title = {The Drosophila formin DAAM regulates the tracheal cuticle pattern through organizing the actin cytoskeleton},
	url = {https://m2.mtmt.hu/api/publication/1914506},
	author = {Matusek, Tamás and Djiane, A and Jankovics, Ferenc and Brunner, D and Mlodzik, M and Mihály, József},
	doi = {10.1242/dev.02266},
	journal-iso = {DEVELOPMENT},
	journal = {DEVELOPMENT},
	volume = {133},
	unique-id = {1914506},
	issn = {0950-1991},
	year = {2006},
	eissn = {1477-9129},
	pages = {957-966}
}

@article{MTMT:1322352,
	title = {Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension},
	url = {https://m2.mtmt.hu/api/publication/1322352},
	author = {Trombitás, Károly and Granzier, H},
	journal-iso = {AM J PHYSIOL CELL PH},
	journal = {AMERICAN JOURNAL OF PHYSIOLOGY: CELL PHYSIOLOGY},
	volume = {273},
	unique-id = {1322352},
	issn = {0363-6143},
	abstract = {The I band of cardiac sarcomeres contains both actin and titin/connectin filaments. Earlier work has suggested that titin binds to actin in situ. This interaction must be weak in the region of the I band where titin behaves elastically. On the other hand, titin may bind strongly to actin in the similar to 100-nm-wide region adjoining the Z line, where titin has been found to be inelastic. To study the putative interaction between titin and actin, techniques for selective removal of actin from different regions of the I band are needed. Here we report studies with a gelsolin fragment (FX-45) and extract actin from rat cardiac myocytes. Actin extraction was biphasic: the majority of actin was extracted in similar to 10 min, whereas actin near the Z line (where titin is inelastic) required a similar to 10-fold longer extraction time. Thus, by controlling the extraction time, we could remove either the full actin filament outside the Z line or just the segment of the actin filament that extends beyond the inelastic region of titin that adjoins the Z line. The actin filament-free I band contained titin filaments, typically with one filament extending from each thick filament. In addition, we observed a dark transverse line (junction line), the location of which in the sarcomere varied linearly with sarcomere length. The position in the sarcomere of the junction line coincided with the binding site of the anti-titin antibody 9D10. Actin removal significantly affected the slack sarcomere length. Slack sarcomere length was 1.85 +/- 0.04 mu m in control cells and decreased to 1.71 +/- 0.05 mu m after actin near the Z line was extracted. This length reduction may be caused by contraction of the titin segment that becomes exposed after actin removal near the Z line, indicating that titin is not only attached to the actin filament but is also under tension.},
	year = {1997},
	eissn = {1522-1563},
	pages = {C662-C670}
}