@article{MTMT:31879664, title = {Condition-dependent functional shift of two Drosophila Mtmr lipid phosphatases in autophagy control}, url = {https://m2.mtmt.hu/api/publication/31879664}, author = {Manzéger, Anna and Tagscherer, Kinga and Lőrincz, Péter and Szaker, Henrik Mihály and Lukácsovich, T and Pliz, P and Kméczik, R and Csikós, György and Erdélyi, Miklós and Sass, Miklós and Kovács, Tibor and Vellai, Tibor and Billes, Viktor András}, doi = {10.1080/15548627.2021.1899681}, journal-iso = {AUTOPHAGY}, journal = {AUTOPHAGY}, volume = {17}, unique-id = {31879664}, issn = {1554-8627}, year = {2021}, eissn = {1554-8635}, pages = {4010-4028}, orcid-numbers = {Manzéger, Anna/0000-0002-3655-8335; Lőrincz, Péter/0000-0001-7374-667X; Szaker, Henrik Mihály/0000-0001-8340-8287; Csikós, György/0000-0002-5881-5363; Sass, Miklós/0000-0002-4559-8216; Kovács, Tibor/0000-0002-0632-9128; Vellai, Tibor/0000-0002-3520-2572; Billes, Viktor András/0000-0003-0030-6221} } @article{MTMT:3399716, title = {Developmentally regulated autophagy is required for eye formation in Drosophila.}, url = {https://m2.mtmt.hu/api/publication/3399716}, author = {Billes, Viktor András and Kovács, Tibor and Manzéger, Anna and Lőrincz, Péter and Vágó-Szincsák, Sára and Regős, Ágnes and Kulcsár, Péter István and Korcsmáros, Tamás and Lukacsovich, T and Hoffmann, Gyula and Erdélyi, Miklós and Mihály, József and Vellainé Takács, Krisztina and Sass, Miklós and Vellai, Tibor}, doi = {10.1080/15548627.2018.1454569}, journal-iso = {AUTOPHAGY}, journal = {AUTOPHAGY}, volume = {14}, unique-id = {3399716}, issn = {1554-8627}, abstract = {The compound eye of the fruit fly Drosophila melanogaster is one of the most intensively studied and best understood model organs in the field of developmental genetics. Herein we demonstrate that autophagy, an evolutionarily conserved selfdegradation process of eukaryotic cells, is essential for eye development in this organism. Autophagic structures accumulate in a specific pattern in the developing eye disc, predominantly in the morphogenetic furrow (MF) and differentiation zone. Silencing of several autophagy genes (Atg) in the eye primordium severely affects the morphology of the adult eye through triggering ectopic cell death. In Atg mutant genetic backgrounds however genetic compensatory mechanisms largely rescue autophagic activity in, and thereby normal morphogenesis of, this organ. We also show that in the eye disc the expression of a key autophagy gene, Atg8a, is controlled in a complex manner by the anterior Hox paralog lab (labial), a master regulator of early development. Atg8a transcription is repressed in front of, while activated along, the MF by lab. The amount of autophagic structures then remains elevated behind the moving MF. These results indicate that eye development in Drosophila depends on the cell death-suppressing and differentiating effects of the autophagic process. This novel, developmentally regulated function of autophagy in the morphogenesis of the compound eye may shed light on a more fundamental role for cellular self-digestion in differentiation and organ formation than previously thought.}, year = {2018}, eissn = {1554-8635}, pages = {1499-1519}, orcid-numbers = {Billes, Viktor András/0000-0003-0030-6221; Kovács, Tibor/0000-0002-0632-9128; Manzéger, Anna/0000-0002-3655-8335; Lőrincz, Péter/0000-0001-7374-667X; Vágó-Szincsák, Sára/0000-0002-3747-5582; Kulcsár, Péter István/0000-0002-7783-5108; Hoffmann, Gyula/0000-0002-2206-6997; Vellainé Takács, Krisztina/0000-0002-4472-0363; Sass, Miklós/0000-0002-4559-8216; Vellai, Tibor/0000-0002-3520-2572} } @article{MTMT:3005853, title = {Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)}, url = {https://m2.mtmt.hu/api/publication/3005853}, author = {Klionsky, DJ and Abdelmohsen, K and Abe, A and Abedin, MJ and Abeliovich, H and Acevedo, Arozena A and Adachi, H 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Armstrong, JL and Arnould, T and Arsov, I and Asanuma, K and Askanas, V and Asselin, E and Atarashi, R and Atherton, SS and Atkin, JD and Attardi, LD and Auberger, P and Auburger, G and Aurelian, L and Autelli, R and Avagliano, L and Avantaggiati, ML and Avrahami, L and Awale, S and Azad, N and Bachetti, T and Backer, JM and Bae, DH and Bae, JS and Bae, ON and Bae, SH and Baehrecke, EH and Baek, SH and Baghdiguian, S and Bagniewska-Zadworna, A and Bai, H and Bai, J and Bai, XY and Bailly, Y and Balaji, KN and Balduini, W and Ballabio, A and Balzan, R and Banerjee, R and Bánhegyi, Gábor and Bao, H and Barbeau, B and Barrachina, MD and Barreiro, E and Bartel, B and Bartolome, A and Bassham, DC and Bassi, MT and Bast, RC Jr and Basu, A and Batista, MT and Batoko, H and Battino, M and Bauckman, K and Baumgarner, BL and Bayer, KU and Beale, R and Beaulieu, JF and Beck, GR Jr and Becker, C and Beckham, JD and Bedard, PA and Bednarski, PJ and Begley, TJ and Behl, C and Behrends, C and 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Cecconi, F and Cederbaum, AI and Cena, V and Cenci, S and Cerella, C and Cervia, D and Cetrullo, S and Chaachouay, H and Chae, HJ and Chagin, AS and Chai, CY and Chakrabarti, G and Chamilos, G and Chan, EY and Chan, MT and Chandra, D and Chandra, P and Chang, CP and Chang, RC and Chang, TY and Chatham, JC and Chatterjee, S and Chauhan, S and Che, Y and Cheetham, ME and Cheluvappa, R and Chen, CJ and Chen, G and Chen, GC and Chen, G and Chen, H and Chen, JW and Chen, JK and Chen, M and Chen, M and Chen, P and Chen, Q and Chen, Q and Chen, SD and Chen, S and Chen, SS and Chen, W and Chen, WJ and Chen, WQ and Chen, W and Chen, X and Chen, YH and Chen, YG and Chen, Y and Chen, Y and Chen, Y and Chen, YJ and Chen, YQ and Chen, Y and Chen, Z and Chen, Z and Cheng, A and Cheng, CH and Cheng, H and Cheong, H and Cherry, S and Chesney, J and Cheung, CH and Chevet, E and Chi, HC and Chi, SG and Chiacchiera, F and Chiang, HL and Chiarelli, R and Chiariello, M and Chieppa, M and Chin, LS and Chiong, M and Chiu, GN and Cho, DH and Cho, SG and Cho, WC and Cho, YY and Cho, YS and Choi, AM and Choi, EJ and Choi, EK and Choi, J and Choi, ME and Choi, SI and Chou, TF and Chouaib, S and Choubey, D and Choubey, V and Chow, KC and Chowdhury, K and Chu, CT and Chuang, TH and Chun, T and Chung, H and Chung, T and Chung, YL and Chwae, YJ and Cianfanelli, V and Ciarcia, R and Ciechomska, IA and Ciriolo, MR and Cirone, M and Claerhout, S and Clague, MJ and Claria, J and Clarke, PG and Clarke, R and Clementi, E and Cleyrat, C and Cnop, M and Coccia, EM and Cocco, T and Codogno, P and Coers, J and Cohen, EE and Colecchia, D and Coletto, L and Coll, NS and Colucci-Guyon, E and Comincini, S and Condello, M and Cook, KL and Coombs, GH and Cooper, CD and Cooper, JM and Coppens, I and Corasaniti, MT and Corazzari, M and Corbalan, R and Corcelle-Termeau, E and Cordero, MD and Corral-Ramos, C and Corti, O and Cossarizza, A and Costelli, P and Costes, S and Cotman, SL and Coto-Montes, A and Cottet, S and Couve, E and Covey, LR and Cowart, LA and Cox, JS and Coxon, FP and Coyne, CB and Cragg, MS and Craven, RJ and Crepaldi, T and Crespo, JL and Criollo, A and Crippa, V and Cruz, MT and Cuervo, AM and Cuezva, JM and Cui, T and Cutillas, PR and Czaja, MJ and Czyzyk-Krzeska, MF and Dagda, RK and Dahmen, U and Dai, C and Dai, W and Dai, Y and Dalby, KN and Dalla, Valle L and Dalmasso, G and D'Amelio, M and Damme, M and Darfeuille-Michaud, A and Dargemont, C and Darley-Usmar, VM and Dasarathy, S and Dasgupta, B and Dash, S and Dass, CR and Davey, HM and Davids, LM and Davila, D and Davis, RJ and Dawson, TM and Dawson, VL and Daza, P and de Belleroche, J and de Figueiredo, P and de Figueiredo, RC and de la, Fuente J and De Martino, L and De Matteis, A and De Meyer, GR and De Milito, A and De Santi, M and de Souza, W and De Tata, V and De Zio, D and Debnath, J and Dechant, R and Decuypere, JP and Deegan, S and Dehay, B and Del Bello, B and Del Re, DP and Delage-Mourroux, R and Delbridge, LM and Deldicque, L and Delorme-Axford, E and Deng, Y and Dengjel, J and Denizot, M and Dent, P and Der, CJ and Deretic, V and Derrien, B and Deutsch, E and Devarenne, TP and Devenish, RJ and Di Bartolomeo, S and Di Daniele, N and Di Domenico, F and Di Nardo, A and Di Paola, S and Di Pietro, A and Di Renzo, L and DiAntonio, A and Diaz-Araya, G and Diaz-Laviada, I and Diaz-Meco, MT and Diaz-Nido, J and Dickey, CA and Dickson, RC and Diederich, M and Digard, P and Dikic, I and Dinesh-Kumar, SP and Ding, C and Ding, WX and Ding, Z and Dini, L and Distler, JH and Diwan, A and Djavaheri-Mergny, M and Dmytruk, K and Dobson, RC and Doetsch, V and Dokladny, K and Dokudovskaya, S and Donadelli, M and Dong, XC and Dong, X and Dong, Z and Donohue, TM Jr and Doran, KS and D'Orazi, G and Dorn, GW nd and Dosenko, V and Dridi, S and Drucker, L and Du, J and Du, LL and Du, L and du, Toit A and Dua, P and Duan, L and Duann, P and Dubey, VK and Duchen, MR and Duchosal, MA and Duez, H and Dugail, I and Dumit, VI and Duncan, MC and Dunlop, EA and Dunn, WA Jr and Dupont, N and Dupuis, L and Duran, RV and Durcan, TM and Duvezin-Caubet, S and Duvvuri, U and Eapen, V and Ebrahimi-Fakhari, D and Echard, A and Eckhart, L and Edelstein, CL and Edinger, AL and Eichinger, L and Eisenberg, T and Eisenberg-Lerner, A and Eissa, NT and El-Deiry, WS and El-Khoury, V and Elazar, Z and Eldar-Finkelman, H and Elliott, CJ and Emanuele, E and Emmenegger, U and Engedal, N and Engelbrecht, AM and Engelender, S and Enserink, JM and Erdmann, R and Erenpreisa, J and Eri, R and Eriksen, JL and Erman, A and Escalante, R and Eskelinen, EL and Espert, L and Esteban-Martinez, L and Evans, TJ and Fabri, M and Fabrias, G and Fabrizi, C and Facchiano, A and Faergeman, NJ and Faggioni, A and Fairlie, WD and Fan, C and Fan, D and Fan, J and Fang, S and Fanto, M and Fanzani, A and Farkas, T and Faure, M and Favier, FB and Fearnhead, H and Federici, M and Fei, E and Felizardo, TC and Feng, H and Feng, Y and Feng, Y and Ferguson, TA and Fernandez, AF and Fernandez-Barrena, MG and Fernandez-Checa, JC and Fernandez-Lopez, A and Fernandez-Zapico, ME and Feron, O and Ferraro, E and Ferreira-Halder, CV and Fésüs, László and Feuer, R and Fiesel, FC and Filippi-Chiela, EC and Filomeni, G and Fimia, GM and Fingert, JH and Finkbeiner, S and Finkel, T and Fiorito, F and Fisher, PB and Flajolet, M and Flamigni, F and Florey, O and Florio, S and Floto, RA and Folini, M and Follo, C and Fon, EA and Fornai, F and Fortunato, F and Fraldi, A and Franco, R and Francois, A and Francois, A and Frankel, LB and Fraser, ID and Frey, N and Freyssenet, DG and Frezza, C and Friedman, SL and Frigo, DE and Fu, D and Fuentes, JM and Fueyo, J and Fujitani, Y and Fujiwara, Y and Fujiya, M and Fukuda, M and Fulda, S and Fusco, C and Gabryel, B and Gaestel, M and Gailly, P and Gajewska, M and Galadari, S and Galili, G and Galindo, I and Galindo, MF and Galliciotti, G and Galluzzi, L and Galluzzi, L and Galy, V and 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Simmet, T and Simon, AK and Simon, HU and Simone, C and Simons, M and Simonsen, A and Singh, R and Singh, SV and Singh, SK and Sinha, D and Sinha, S and Sinicrope, FA and Sirko, A and Sirohi, K and Sishi, BJ and Sittler, A and Siu, PM and Sivridis, E and Skwarska, A and Slack, R and Slaninova, I and Slavov, N and Smaili, SS and Smalley, KS and Smith, DR and Soenen, SJ and Soleimanpour, SA and Solhaug, A and Somasundaram, K and Son, JH and Sonawane, A and Song, C and Song, F and Song, HK and Song, JX and Song, W and Soo, KY and Sood, AK and Soong, TW and Soontornniyomkij, V and Sorice, M and Sotgia, F and Soto-Pantoja, DR and Sotthibundhu, A and Sousa, MJ and Spaink, HP and Span, PN and Spang, A and Sparks, JD and Speck, PG and Spector, SA and Spies, CD and Springer, W and Clair, DS and Stacchiotti, A and Staels, B and Stang, MT and Starczynowski, DT and Starokadomskyy, P and Steegborn, C and Steele, JW and Stefanis, L and Steffan, J and Stellrecht, CM and Stenmark, H and Stepkowski, TM and Stern, ST and Stevens, C and Stockwell, BR and Stoka, V and Storchova, Z and Stork, B and Stratoulias, V and Stravopodis, DJ and Strnad, P and Strohecker, AM and Strom, AL and Stromhaug, P and Stulik, J and Su, YX and Su, Z and Subauste, CS and Subramaniam, S and Sue, CM and Suh, SW and Sui, X and Sukseree, S and Sulzer, D and Sun, FL and Sun, J and Sun, J and Sun, SY and Sun, Y and Sun, Y and Sun, Y and Sundaramoorthy, V and Sung, J and Suzuki, H and Suzuki, K and Suzuki, N and Suzuki, T and Suzuki, YJ and Swanson, MS and Swanton, C and Sward, K and Swarup, G and Sweeney, ST and Sylvester, PW and Szatmári, Zsuzsanna and Szegezdi, E and Szlosarek, PW and Taegtmeyer, H and Tafani, M and Taillebourg, E and Tait, SW and Vellainé Takács, Krisztina and Takahashi, Y and Takáts, Szabolcs and Takemura, G and Takigawa, N and Talbot, NJ and Tamagno, E and Tamburini, J and Tan, CP and Tan, L and Tan, ML and Tan, M and Tan, YJ and Tanaka, K and Tanaka, M and Tang, D and Tang, D and Tang, G and Tanida, I and Tanji, K and Tannous, BA and Tapia, JA and Tasset-Cuevas, I and Tatar, M and Tavassoly, I and Tavernarakis, N and Taylor, A and Taylor, GS and Taylor, GA and Taylor, JP and Taylor, MJ and Tchetina, EV and Tee, AR and Teixeira-Clerc, F and Telang, S and Tencomnao, T and Teng, BB and Teng, RJ and Terro, F and Tettamanti, G and Theiss, AL and Theron, AE and Thomas, KJ and Thome, MP and Thomes, PG and Thorburn, A and Thorner, J and Thum, T and Thumm, M and Thurston, TL and Tian, L and Till, A and Ting, JP and Titorenko, VI and Toker, L and Toldo, S and Tooze, SA and Topisirovic, I and Torgersen, ML and Torosantucci, L and Torriglia, A and Torrisi, MR and Tournier, C and Towns, R and Trajkovic, V and Travassos, LH and Triola, G and Tripathi, DN and Trisciuoglio, D and Troncoso, R and Trougakos, IP and Truttmann, AC and Tsai, KJ and Tschan, MP and Tseng, YH and Tsukuba, T and Tsung, A and Tsvetkov, AS and Tu, S and Tuan, HY and Tucci, M and Tumbarello, DA and Turk, B and Turk, V and Turner, RF and Tveita, AA and Tyagi, SC and Ubukata, M and Uchiyama, Y and Udelnow, A and Ueno, T and Umekawa, M and Umemiya-Shirafuji, R and Underwood, BR and Ungermann, C and Ureshino, RP and Ushioda, R and Uversky, VN and Uzcategui, NL and Vaccari, T and Vaccaro, MI and Vachova, L and Vakifahmetoglu-Norberg, H and Valdor, R and Valente, EM and Vallette, F and Valverde, AM and Van, den Berghe G and Van, Den Bosch L and van den Brink, GR and van der Goot, FG and van der Klei, IJ and van der Laan, LJ and van Doorn, WG and van Egmond, M and van Golen, KL and Van, Kaer L and van Lookeren, Campagne M and Vandenabeele, P and Vandenberghe, W and Vanhorebeek, I and Varela-Nieto, I and Vasconcelos, MH and Vasko, R and Vavvas, DG and Vega-Naredo, I and Velasco, G and Velentzas, AD and Velentzas, PD and Vellai, Tibor and Vellenga, E and Vendelbo, MH and Venkatachalam, K and Ventura, N and Ventura, S and Veras, PS and Verdier, M and Vértessy, Beáta (Grolmuszné) and Viale, A and Vidal, M 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Yamanaka, K and Yamashina, S and Yamashiro, S and Yan, B and Yan, B and Yan, X and Yan, Z and Yanagi, Y and Yang, DS and Yang, JM and Yang, L and Yang, M and Yang, PM and Yang, P and Yang, Q and Yang, W and Yang, WY and Yang, X and Yang, Y and Yang, Y and Yang, Z and Yang, Z and Yao, MC and Yao, PJ and Yao, X and Yao, Z and Yao, Z and Yasui, LS and Ye, M and Yedvobnick, B and Yeganeh, B and Yeh, ES and Yeyati, PL and Yi, F and Yi, L and Yin, XM and Yip, CK and Yoo, YM and Yoo, YH and Yoon, SY and Yoshida, KI and Yoshimori, T and Young, KH and Yu, H and Yu, JJ and Yu, JT and Yu, J and Yu, L and Yu, WH and Yu, XF and Yu, Z and Yuan, J and Yuan, ZM and Yue, BY and Yue, J and Yue, Z and Zacks, DN and Zacksenhaus, E and Zaffaroni, N and Zaglia, T and Zakeri, Z and Zecchini, V and Zeng, J and Zeng, M and Zeng, Q and Zervos, AS and Zhang, DD and Zhang, F and Zhang, G and Zhang, GC and Zhang, H and Zhang, H and Zhang, H and Zhang, H and Zhang, J and Zhang, J and Zhang, J and Zhang, J and Zhang, JP and Zhang, L and Zhang, L and Zhang, L and Zhang, L and Zhang, MY and Zhang, X and Zhang, XD and Zhang, Y and Zhang, Y and Zhang, Y and Zhang, Y and Zhang, Y and Zhao, M and Zhao, WL and Zhao, X and Zhao, YG and Zhao, Y and Zhao, Y and Zhao, YX and Zhao, Z and Zhao, ZJ and Zheng, D and Zheng, XL and Zheng, X and Zhivotovsky, B and Zhong, Q and Zhou, GZ and Zhou, G and Zhou, H and Zhou, SF and Zhou, XJ and Zhu, H and Zhu, H and Zhu, WG and Zhu, W and Zhu, XF and Zhu, Y and Zhuang, SM and Zhuang, X and Ziparo, E and Zois, CE and Zoladek, T and Zong, WX and Zorzano, A and Zughaier, SM}, doi = {10.1080/15548627.2015.1100356}, journal-iso = {AUTOPHAGY}, journal = {AUTOPHAGY}, volume = {12}, unique-id = {3005853}, issn = {1554-8627}, year = {2016}, eissn = {1554-8635}, pages = {1-222}, orcid-numbers = {Bánhegyi, Gábor/0000-0001-7559-0066; Billes, Viktor András/0000-0003-0030-6221; Juhász, Gábor/0000-0001-8548-8874; Kapuy, Orsolya/0000-0002-8484-4504; Kovács, Tibor/0000-0002-0632-9128; Lőrincz, Péter/0000-0001-7374-667X; Margittai, Éva/0000-0003-0841-0613; Nagy, Péter/0000-0002-5053-0646; Orosz, László/0000-0002-5268-6134; Sass, Miklós/0000-0002-4559-8216; Vellainé Takács, Krisztina/0000-0002-4472-0363; Takáts, Szabolcs/0000-0003-2139-7740; Vellai, Tibor/0000-0002-3520-2572} } @article{MTMT:3097625, title = {Guidelines for the Use and Interpretation of Assays for Monitoring Autophagy (3rd edition) (vol 12, pg 1, 2015)}, url = {https://m2.mtmt.hu/api/publication/3097625}, author = {Klionsky, D and Abeliovich, H and Agostinis, P and Agrawal, DK and Aliev, G and Askew, DS and Baba, M and Baehrecke, EH and Bahr, BA and Ballabio, A and Bamber, BA and Bassham, DC and Bergamini, E and Bi, X and Biard-Piechaczyk, M and Blum, JS and Bredesen, DE and Brodsky, JL and Brumell, JH and Brunk, UT and Bursch, W and Camougrand, N and Cebollero, E and Cecconi, F and Chen, Y and Chin, L-S and Choi, A and Chu, CT and Chung, J and Clarke, PGH and Clark, RSB and Clarke, SG and Clavé, C and Cleveland, JL and Codogno, P and Colombo, MI and Cotomontes, A and Cregg, JM and Cuervo, AM and Debnath, J and Demarchi, F and Dennis, PB and Dennis, PA and Deretic, V and Devenish, RJ and Di Sano, F and Dice, JF and DiFiglia, M and Dinesh-Kumar, S and Distelhorst, CW and Djavaheri-Mergny, M and Dorsey, FC and Dröge, W and Dron, M and Dunn, Jr WA and Duszenko, M and Eissa, NT and Elazar, Z and Esclatine, A and Eskelinen, E-L and Fésüs, László and Finley, KD and Fuentes, JM and Fueyo, J and Fujisaki, K and Galliot, B and Gao, F-B and Gewirtz, DA and Gibson, SB and Gohla, A and Goldberg, AL and Gonzalez, R and González-Estévez, C and Gorski, S and Gottlieb, RA and Häussinger, D and He, Y-W and Heidenreich, K and Hill, JA and Høyer-Hansen, M and Hu, X and Huang, W-P and Iwasaki, A and Jäättelä, M and Jackson, WT and Jiang, X and Jin, S and Johansen, T and Jung, JU and Kadowaki, M and Kang, C and Kelekar, A and Kessel, DH and Kiel, JAKW and Hong, PK and Kimchi, A and Kinsella, TJ and Kiselyov, K and Kitamoto, K and Knecht, E and Komatsu, M and Kominami, E and Kondo, S and Kovács, AL and Kroemer, G and Kuan, C-Y and Kumar, R and Kundu, M and Landry, J and Laporte, M and Le, W and Lei, H-Y and Lenardo, MJ and Levine, B and Lieberman, A and Lim, K-L and Lin, F-C and Liou, W and Liu, LF and Lopez-Berestein, G and López-Otín, C and Lu, B and Macleod, KF and Malorni, W and Martinet, W and Matsuoka, K and Mautner, J and Meijer, AJ and Meléndez, A and Michels, P and Miotto, G and Mistiaen, WP and Mizushima, N and Mograbi, B and Monastyrska, I and Moore, MN and Moreira, PI and Moriyasu, Y and Motyl, T and Münz, C and Murphy, LO and Naqvi, NI and Neufeld, TP and Nishino, I and Nixon, RA and Noda, T and Nürnberg, B and Ogawa, M and Oleinick, NL and Olsen, LJ and Ozpolat, B and Paglin, S and Palmer, GE and Papassideri, I and Parkes, M and Perlmutter, DH and Perry, G and Piacentini, M and Pinkas-Kramarski, R and Prescott, M and Proikascezanne, T and Raben, N and Rami, A and Reggiori, F and Rohrer, B and Rubinsztein, DC and Ryan, KM and Sadoshima, J and Sakagami, H and Sakai, Y and Sandri, M and Sasakawa, C and Sass, Miklós and Schneider, C and Seglen, PO and Seleverstov, O and Settleman, J and Shacka, JJ and Shapiro, IM and Sibirny, A and Silva-Zacarin, ECM and Simon, H-U and Simone, C and Simonsen, A and Smith, MA and Spanel-Borowski, K and Srinivas, V and Steeves, M and Stenmark, H and Stromhaug, PE and Subauste, CS and Sugimoto, S and Sulzer, D and Suzuki, T and Swanson, MS and Tabas, I and Takeshita, F and Talbot, NJ and Tallóczy, Z and Tanaka, K and Tanaka, K and Tanida, I and Taylor, GS and Taylor, JP and Terman, A and Tettamanti, G and Thompson, CB and Thumm, M and Tolkovsky, AM and Tooze, SA and Truant, R and Tumanovska, LV and Uchiyama, Y and Ueno, T and Uzcátegui, NL and Van, Der Klei I and Vaquero, EC and Vellai, Tibor and Vogel, MW and Wang, H-G and Webster, P and Wiley, JW and Xi, Z and Xiao, G and Yahalom, J and Yang, J-M and Yap, G and Yin, X-M and Yoshimori, T and Yu, L and Yue, Z and Yuzaki, M and Zabirnyk, O and Zheng, X and Zhu, X and Deter, RL}, doi = {10.1080/15548627.2016.1147886}, journal-iso = {AUTOPHAGY}, journal = {AUTOPHAGY}, volume = {12}, unique-id = {3097625}, issn = {1554-8627}, keywords = {ERROR; erratum}, year = {2016}, eissn = {1554-8635}, pages = {443-443}, orcid-numbers = {Sass, Miklós/0000-0002-4559-8216; Vellai, Tibor/0000-0002-3520-2572} } @article{MTMT:2924262, title = {Retromer ensures the degradation of autophagic cargo via maintaining lysosome function in Drosophila.}, url = {https://m2.mtmt.hu/api/publication/2924262}, author = {Maruzs, Tamás and Lőrincz, Péter and Szatmári, Zsuzsanna and Széplaki, Szilvia and Sándor, Zoltán and Lakatos, Zsolt and Puska, Gina and Juhász, Gábor and Sass, Miklós}, doi = {10.1111/tra.12309}, journal-iso = {TRAFFIC}, journal = {TRAFFIC}, volume = {16}, unique-id = {2924262}, issn = {1398-9219}, abstract = {The retromer is an evolutionarily conserved coat complex that consists of Vps26, Vps29, Vps35 and a heterodimer of sorting nexin (Snx) protein in yeast. Retromer mediates the recycling of transmembrane proteins from endosomes to the trans-Golgi network, including receptors that are essential for the delivery of hydrolytic enzymes to lysosomes. Besides its function in lysosomal enzyme receptor recycling, involvement of retromer has also been proposed in a variety of vesicular trafficking events, including early steps of autophagy and endocytosis. Here we show that the late stages of autophagy and endocytosis are impaired in Vps26 and Vps35 deficient Drosophila larval fat body cells, but formation of autophagosomes and endosomes is not compromised. Accumulation of aberrant autolysosomes and amphisomes in the absence of retromer function appears to be the consequence of decreased degradative capacity, as they contain undigested cytoplasmic material. Accordingly, we show that retromer is required for proper cathepsin L trafficking mainly independent of LERP, the Drosophila homolog of the cation-independent mannose 6-phosphate receptor. Finally, we find that Snx3 and Snx6 are also required for proper autolysosomal degradation in Drosophila larval fat body cells.}, year = {2015}, eissn = {1600-0854}, pages = {1088-1107}, orcid-numbers = {Maruzs, Tamás/0000-0001-8142-3221; Lőrincz, Péter/0000-0001-7374-667X; Puska, Gina/0009-0002-0710-602X; Juhász, Gábor/0000-0001-8548-8874; Sass, Miklós/0000-0002-4559-8216} } @article{MTMT:2941631, title = {Specialized Cortex Glial Cells Accumulate Lipid Droplets in Drosophila melanogaster}, url = {https://m2.mtmt.hu/api/publication/2941631}, author = {Kis, Viktor and Barti, Benjámin and Lippai, Mónika and Sass, Miklós}, doi = {10.1371/journal.pone.0131250}, journal-iso = {PLOS ONE}, journal = {PLOS ONE}, volume = {10}, unique-id = {2941631}, abstract = {Lipid droplets (LDs) are common organelles of the majority of eukaryotic cell types. Their biological significance has been extensively studied in mammalian liver cells and white adipose tissue. Although the central nervous system contains the highest relative amount and the largest number of different lipid species, neither the spatial nor the temporal distribution of LDs has been described. In this study, we used the brain of the fruitfly, Drosophila melanogaster, to investigate the neuroanatomy of LDs. We demonstrated that LDs are exclusively localised in glial cells but not in neurons in the larval nervous system. We showed that the brain's LD pool, rather than being constant, changes dynamically during development and reaches its highest value at the beginning of metamorphosis. LDs are particularly enriched in cortex glial cells located close to the brain surface. These specialized superficial cortex glial cells contain the highest amount of LDs among glial cell types and encapsulate neuroblasts and their daughter cells. Superficial cortex glial cells, combined with subperineurial glial cells, express the Drosophila fatty acid binding protein (Dfabp), as we have demonstrated through light-and electron microscopic immunocytochemistry. To the best of our best knowledge this is the first study that describes LD neuroanatomy in the Drosophila larval brain.}, year = {2015}, eissn = {1932-6203}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233; Sass, Miklós/0000-0002-4559-8216} } @CONFERENCE{MTMT:3079696, title = {Retromer is required for autophagy through maintaining proper lysosome function in Drosophila}, url = {https://m2.mtmt.hu/api/publication/3079696}, author = {Maruzs, Tamás and Lőrincz, Péter and Szatmári, Zsuzsanna and Széplaki, Szilvia and Sándor, Zoltán and Lakatos, Zsolt and Puska, Gina and Juhász, Gábor and Sass, Miklós}, booktitle = {24th European Drosophila Research Conference (EDRC) 2015}, unique-id = {3079696}, year = {2015}, pages = {308}, orcid-numbers = {Maruzs, Tamás/0000-0001-8142-3221; Lőrincz, Péter/0000-0001-7374-667X; Puska, Gina/0009-0002-0710-602X; Juhász, Gábor/0000-0001-8548-8874; Sass, Miklós/0000-0002-4559-8216} } @CONFERENCE{MTMT:3081072, title = {Developmental autophagy is required for eye patterning in Drosophila}, url = {https://m2.mtmt.hu/api/publication/3081072}, author = {Billes, Viktor András and Kovács, Tibor and Lőrincz, Péter and Ágnes, Regős and Manzéger, Anna and Sára, Szincsák and Miklós, Erdélyi and József, Mihály and Sass, Miklós and Tibor, Vellai}, booktitle = {Hungarian Molecular Life Sciences 2015}, unique-id = {3081072}, year = {2015}, pages = {71-71}, orcid-numbers = {Billes, Viktor András/0000-0003-0030-6221; Kovács, Tibor/0000-0002-0632-9128; Lőrincz, Péter/0000-0001-7374-667X; Manzéger, Anna/0000-0002-3655-8335; Sass, Miklós/0000-0002-4559-8216} } @article{MTMT:2459378, title = {Autophagy is required for zebrafish caudal fin regeneration}, url = {https://m2.mtmt.hu/api/publication/2459378}, author = {Varga, Máté and Sass, Miklós and Papp, Diána and Vellainé Takács, Krisztina and Kobolák, Julianna and Dinnyés, András and Klionsky, DJ and Vellai, Tibor}, doi = {10.1038/cdd.2013.175}, journal-iso = {CELL DEATH DIFFER}, journal = {CELL DEATH AND DIFFERENTIATION}, volume = {21}, unique-id = {2459378}, issn = {1350-9047}, keywords = {CELLS; DIFFERENTIATION; MECHANISMS; ZEBRAFISH; PROLIFERATION; regeneration; Cell Death; Autophagy; Osteoblasts; dedifferentiation; MONITORING AUTOPHAGY; SELF-DIGESTION; BLASTEMA; HEART REGENERATION}, year = {2014}, eissn = {1476-5403}, pages = {547-556}, orcid-numbers = {Varga, Máté/0000-0003-4289-1705; Sass, Miklós/0000-0002-4559-8216; Vellainé Takács, Krisztina/0000-0002-4472-0363; Kobolák, Julianna/0000-0002-0986-9517; Vellai, Tibor/0000-0002-3520-2572} } @article{MTMT:2483302, title = {Rab11 facilitates crosstalk between autophagy and endosomal pathway through regulation of Hook localization.}, url = {https://m2.mtmt.hu/api/publication/2483302}, author = {Szatmári, Zsuzsanna and Kis, Viktor and Lippai, Mónika and Hegedűs, Krisztina and Faragó, Tamás and Lőrincz, Péter and Tanaka, T and Juhász, Gábor and Sass, Miklós}, doi = {10.1091/mbc.E13-10-0574}, journal-iso = {MOL BIOL CELL}, journal = {MOLECULAR BIOLOGY OF THE CELL}, volume = {25}, unique-id = {2483302}, issn = {1059-1524}, abstract = {During autophagy, double-membrane autophagosomes deliver sequestered cytoplasmic content to late endosomes and lysosomes for degradation. The molecular mechanism of autophagosome maturation is still poorly characterized. The small GTPase Rab11 regulates endosomal traffic, and is thought to function at the level of recycling endosomes. Here we show that loss of Rab11 leads to accumulation of autophagosomes and late endosomes in Drosophila melanogaster. Rab11 translocates from recycling endosomes to autophagosomes in response to autophagy induction, and physically interacts with Hook, a negative regulator of endosome maturation. Hook anchors endosomes to microtubules, and we show that Rab11 facilitates the fusion of endosomes and autophagosomes by removing Hook from mature late endosomes and inhibiting its homodimerization. Thus, induction of autophagy appears to promote autophagic flux by increased convergence with the endosomal pathway.}, year = {2014}, eissn = {1939-4586}, pages = {522-531}, orcid-numbers = {Lippai, Mónika/0000-0002-7307-4233; Faragó, Tamás/0000-0001-5987-2629; Lőrincz, Péter/0000-0001-7374-667X; Juhász, Gábor/0000-0001-8548-8874; Sass, Miklós/0000-0002-4559-8216} }