The DOI matches its Crossref record; 110 of the 110 references it cites were found in a registry or an index.
Autophagy and microtubules - new story, old players
Abstract
Summary: Both at a basal level and after induction (especially in response to nutrient starvation), the function of autophagy is to allow cells to degrade and recycle damaged organelles, proteins and other biological constituents. Here, we focus on the role microtubules have in autophagosome formation, autophagosome transport across the cytoplasm and in the formation of autolysosomes. Recent insights into the exact relationship between autophagy and microtubules now point to the importance of microtubule dynamics, tubulin post-translational modifications and microtubule motors in the autophagy process. Such factors regulate signaling pathways that converge to stimulate autophagosome formation. They also orchestrate the movements of pre-autophagosomal structures and autophagosomes or more globally organize and localize immature and mature autophagosomes and lysosomes. Most of the factors that now appear to link microtubules to autophagosome formation or to autophagosome dynamics and fate were identified initially without the notion that sequestration, recruitment and/or interaction with microtubules contribute to their function. Spatial and temporal coordination of many stages in the life of autophagosomes thus underlines the integrative role of microtubules and progressively reveals hidden parts of the autophagy machinery.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Post-translational modifications of tubulin such as acetylation and tyrosination/detyrosination can act either singly or in concert with other modifications to control motor recruitment in a cargo-specific manner (Hammond et al., 2008; Mackeh et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Mackeh et al., 2013
Citations
Cites
1 retracted
Acharya, B. R., Bhattacharyya, S., Choudhury, D., & Chakrabarti, G. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0613-1 · Cited by 69
RetractedAMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Autophagy: Renovation of Cells and Tissues
Mizushima, N., & Komatsu, M. (2011) · Cell · doi:10.1016/j.cell.2011.10.026 · Cited by 6,615
Microtubules as a target for anticancer drugs
Jordan, M. A., & Wilson, L. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1317 · Cited by 4,000
Levine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,728
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506
Dynamic instability of microtubule growth
Mitchison, T., & Kirschner, M. (1984) · Nature · doi:10.1038/312237a0 · Cited by 3,337
The Role of Atg Proteins in Autophagosome Formation
Mizushima, N., Yoshimori, T., & Ohsumi, Y. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154005 · Cited by 2,978
MICROTUBULE POLYMERIZATION DYNAMICS
Desai, A. B., & Mitchison, T. J. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.83 · Cited by 2,660
The Beclin 1 network regulates autophagy and apoptosis
Kang, R., Zeh, H. J., Lotze, M. T., & Tang, D. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.191 · Cited by 2,485
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · cited 2×
“Another pathway that controls autophagy in response to amino acids involves the Rag GTPase, which allows the recruitment of mTOR at the lysosomal membrane, where its direct activators reside (Sancak et al., 2010).”
BackgroundHDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Autophagosome formation: core machinery and adaptations
Xie, Z., & Klionsky, D. J. (2007) · Nature Cell Biology · doi:10.1038/ncb1007-1102 · Cited by 2,237
Rubinsztein, D. C., Mariño, G., & Kroemer, G. (2011) · Cell · doi:10.1016/j.cell.2011.07.030 · Cited by 2,107
ULK-Atg13-FIP200 Complexes Mediate mTOR Signaling to the Autophagy Machinery
Jung, C. H., Jun, C. B., Ro, S.-H., Kim, Y.-M., Otto, N. M., Cao, J., Kundu, M., & Kim, D.-H. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-12-1249 · Cited by 2,025
Mammalian autophagy: core molecular machinery and signaling regulation
Yang, Z., & Klionsky, D. J. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.014 · Cited by 1,956
Axe, E. L., Walker, S. A., Manifava, M., Chandra, P., Roderick, H. L., Habermann, A., Griffiths, G., & Ktistakis, N. T. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803137 · Cited by 1,885
Regulation of Mammalian Autophagy in Physiology and Pathophysiology
Ravikumar, B., Sarkar, S., Davies, J. E., Futter, M., García-Arencibia, M., Green-Thompson, Z. W., Jiménez-Sánchez, M., Korolchuk, V. I., Lichtenberg, M., Luo, S., et al. (2010) · Physiological Reviews · doi:10.1152/physrev.00030.2009 · Cited by 1,789
Microtubule nucleation by γ-tubulin complexes
Kollman, J. M., Merdes, A., Mourey, L., & Agard, D. A. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3209 · Cited by 1,583
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542
Kawaguchi, Y., Kovacs, J. J., McLaurin, A. C., Vance, J. M., Ito, A., & Yao, T. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,529
Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks
Alers, S., Löffler, A. S., Wesselborg, S., & Stork, B. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06159-11 · Cited by 1,483
Autophagy modulation as a potential therapeutic target for diverse diseases
Rubinsztein, D. C., Codogno, P., & Levine, B. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3802 · Cited by 1,464
Self-citationJNK1-Mediated Phosphorylation of Bcl-2 Regulates Starvation-Induced Autophagy
Wei, Y., Pattingre, S., Sinha, S., Bassik, M., & Levine, B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.001 · Cited by 1,329
Regulation of the mTOR Complex 1 Pathway by Nutrients, Growth Factors, and Stress
Sengupta, S., Peterson, T. R., & Sabatini, D. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.026 · Cited by 1,275
HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS.
Pandey, U. B., Nie, Z., Batlevi, Y., McCray, B. A., Ritson, G. P., Nedelsky, N. B., Schwartz, S. L., DiProspero, N. A., Knight, M. A., Schuldiner, O., et al. (2007) · Nature · doi:10.1038/nature05853 · Cited by 1,234
The Atg12-Atg5 Conjugate Has a Novel E3-like Activity for Protein Lipidation in Autophagy
Hanada, T., Noda, N. N., Satomi, Y., Ichimura, Y., Fujioka, Y., Takao, T., Inagaki, F., & Ohsumi, Y. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700195200 · Cited by 1,123 · cited 2×
“Both contribute to the expansion and the closure of the vesicle in concert with two ubiquitin-like conjugation systems, resulting in the ATG12–ATG5-ATG16L complex and the phosphatidylethanolamine (PtdEtn) conjugate of microtubuleassociated protein 1 light chain 3 [LC3 (MLP3); the mammalian ortholog of Atg8 in budding…”
BackgroundThe Atg16L Complex Specifies the Site of LC3 Lipidation for Membrane Biogenesis in Autophagy
Fujita, N., Itoh, T., Omori, H., Fukuda, M., Noda, T., & Yoshimori, T. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1257 · Cited by 1,123
A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
Hayashi-Nishino, M., Fujita, N., Noda, T., Yamaguchi, A., Yoshimori, T., & Yamamoto, A. (2009) · Nature Cell Biology · doi:10.1038/ncb1991 · Cited by 1,083
The role of the Atg1/ULK1 complex in autophagy regulation
Mizushima, N. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.004 · Cited by 1,062
Role for Rab7 in maturation of late autophagic vacuoles
Jäger, S., Bucci, C., Tanida, I., Ueno, T., Kominami, E., Säftig, P., & Eskelinen, E. (2004) · Journal of Cell Science · doi:10.1242/jcs.01370 · Cited by 970
Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice
Tanaka, Y., Guhde, G., Suter, A., Eskelinen, E.-L., Hartmann, D., Lüllmann-Rauch, R., Janssen, P. M. L., Blanz, J., von Figura, K., & Saftig, P. (2000) · Nature · doi:10.1038/35022595 · Cited by 925
Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
Reed, N. A., Cai, D., Blasius, T. L., Jih, G. T., Meyhofer, E., Gaertig, J., & Verhey, K. J. (2006) · Current Biology · doi:10.1016/j.cub.2006.09.014 · Cited by 919
Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions
Janke, C., & Bulinski, J. C. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3227 · Cited by 896
Autophagy, Immunity, and Microbial Adaptations
Deretic, V. P., & Levine, B. (2009) · Cell Host & Microbe · doi:10.1016/j.chom.2009.05.016 · Cited by 892
Lysosomal positioning coordinates cellular nutrient responses
Korolchuk, V. I., Saiki, S., Lichtenberg, M., Siddiqi, F. H., Roberts, E. A., Imarisio, S., Jahreiss, L., Sarkar, S., Futter, M., Menzies, F. M., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2204 · Cited by 891
The Beclin 1–VPS34 complex – at the crossroads of autophagy and beyond
Funderburk, S. F., Wang, Q. J., & Yue, Z. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.03.002 · Cited by 804
Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelières, F. P., King, S. J., Humbert, S., & Saudou, F. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0037-07.2007 · Cited by 792
Autophagy in the Cellular Energetic Balance
Singh, R., & Cuervo, A. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.004 · Cited by 788
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740 · cited 5×
“The level of tubulin acetylation depends on the histone deacetylase HDAC6 and the NAD-dependent protein deacetylase sirtuin-2 (SIRT2) (Hubbert et al., 2002; North et al., 2003; Zhang et al., 2003), which have also been shown to active mTOR Lysosome Microtubules Omegasome Centrosome Nucleus Kinesins Kif1Bβ Kif2A Format…”
BackgroundInfluential3D tomography reveals connections between the phagophore and endoplasmic reticulum
Ylä‐Anttila, P., Vihinen, H., Jokitalo, E., & Eskelinen, E. (2009) · Autophagy · doi:10.4161/auto.5.8.10274 · Cited by 714
Polson, H. E. J., de Lartigue, J., Rigden, D. J., Reedijk, M., Urbé, S., Clague, M. J., & Tooze, S. A. (2010) · Autophagy · doi:10.4161/auto.6.4.11863 · Cited by 712
Chen, Y., McMillan‐Ward, E., Kong, J., Israels, S. J., & Gibson, S. B. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402233 · Cited by 687
Pankiv, S., Alemu, E. A., Brech, A., Bruun, J., Lamark, T., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200907015 · Cited by 684
Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
Gutierrez, M. G., Munafó, D. B., Berón, W., & Colombo, M. I. (2004) · Journal of Cell Science · doi:10.1242/jcs.01114 · Cited by 680
Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity
Zhao, Y., Yang, J. H., Liao, W., Liu, X., Zhang, H., Wang, S., Wang, D., Feng, J., Yu, L., & Zhu, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2069 · Cited by 632
Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules
Verhey, K. J., Meyer, D., Deehan, R., Blenis, J., Schnapp, B. J., Rapoport, T. A., & Margolis, B. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.5.959 · Cited by 609
Orsi, A., Razi, M., Dooley, H. C., Robinson, D. J., Weston, A., Collinson, L., & Tooze, S. A. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-09-0746 · Cited by 607
Zalckvar, E., Berissi, H., Mizrachy, L., Idelchuk, Y., Koren, I., Eisenstein, M., Sabanay, H., Pinkas‐Kramarski, R., & Kimchi, A. (2009) · The EMBO Reports · doi:10.1038/embor.2008.246 · Cited by 592
mDia mediates Rho-regulated formation and orientation of stable microtubules
Palazzo, A. F., Cook, T. A., Alberts, A. S., & Gundersen, G. G. (2001) · Nature Cell Biology · doi:10.1038/35087035 · Cited by 582
The dynamic interaction of AMBRA1 with the dynein motor complex regulates mammalian autophagy
Bartolomeo, S. D., Corazzari, M., Nazio, F., Oliverio, S., Lisi, G., Antonioli, M., Pagliarini, V., Matteoni, S., Fuoco, C., Giunta, L., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002100 · Cited by 561
Lee, J., Nagano, Y., Taylor, J. P., Lim, K. L., & Yao, T. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001039 · Cited by 545
Overview of macroautophagy regulation in mammalian cells
Mehrpour, M., Esclatine, A., Beau, I., & Codogno, P. (2010) · Cell Research · doi:10.1038/cr.2010.82 · Cited by 516
Self-citationAtg101, a novel mammalian autophagy protein interacting with Atg13
Hosokawa, N., Sasaki, T., Iemura, S.-I., Natsume, T., Hara, T., & Mizushima, N. (2009) · Autophagy · doi:10.4161/auto.5.7.9296 · Cited by 515
Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606077 · Cited by 505
Asymmetric CLASP-Dependent Nucleation of Noncentrosomal Microtubules at the trans-Golgi Network
Efimov, A., Kharitonov, A., Efimova, N., Lončarek, J., Miller, P. M., Andreyeva, N., Gleeson, P. A., Galjart, N., Maia, A. R. R., McLeod, I. X., et al. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.04.002 · Cited by 498
The Itinerary of Autophagosomes: From Peripheral Formation to Kiss‐and‐Run Fusion with Lysosomes
Jahreiss, L., Menzies, F. M., & Rubinsztein, D. C. (2008) · Traffic · doi:10.1111/j.1600-0854.2008.00701.x · Cited by 490
Microtubules Facilitate Autophagosome Formation and Fusion of Autophagosomes with Endosomes
Köchl, R., Hu, X. W., Chan, E. Y. W., & Tooze, S. A. (2005) · Traffic · doi:10.1111/j.1600-0854.2005.00368.x · Cited by 458
Dynein-dependent Movement of Autophagosomes Mediates Efficient Encounters with Lysosomes
Kimura, S., Noda, T., & Yoshimori, T. (2008) · Cell Structure and Function · doi:10.1247/csf.08005 · Cited by 438
Dynein mutations impair autophagic clearance of aggregate-prone proteins
Ravikumar, B., Acevedo-Arozena, A., Imarisio, S., Berger, Z., Vacher, C., O'Kane, C. J., Brown, S. D. M., & Rubinsztein, D. C. (2005) · Nature Genetics · doi:10.1038/ng1591 · Cited by 416
Microtubules and signal transduction
Gundersen, G. G., & Cook, T. A. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80010-6 · Cited by 407
Autophagosome Precursor Maturation Requires Homotypic Fusion
Moreau, K., Ravikumar, B., Renna, M., Puri, C., & Rubinsztein, D. C. (2011) · Cell · doi:10.1016/j.cell.2011.06.023 · Cited by 398
Organization of organelles and membrane traffic by microtubules
Cole, N. B., & Lippincott‐Schwartz, J. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80045-x · Cited by 330
The Golgi Complex Is a Microtubule-organizing Organelle
Chabin-Brion, K., Marceiller, J., Perez, F., Settegrana, C., Drechou, A., Durand, G., & Poüs, C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.7.2047 · Cited by 319
Self-citationMitosis is not a key target of microtubule agents in patient tumors
Komlodi-Pasztor, E., Sackett, D., Wilkerson, J., & Fojo, T. (2011) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.228 · Cited by 314 · cited 1×
“However, human tumour cells divide more slowly than cultured cell lines and tumour cells in animal models (for a review, see Komlodi-Pasztor et al., 2011).”
BackgroundDetection of GTP-Tubulin Conformation in Vivo Reveals a Role for GTP Remnants in Microtubule Rescues
Dimitrov, A., Quesnoit, M., Moutel, S., Cantaloube, I., Poüs, C., & Perez, F. (2008) · Science · doi:10.1126/science.1165401 · Cited by 313
Self-citationSingle molecule imaging reveals differences in microtubule track selection between Kinesin motors
Cai, D., McEwen, D. P., Martens, J. R., Meyhofer, E., & Verhey, K. J. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000216 · Cited by 300
Miller, P. M., Folkmann, A. W., Maia, A. R. R., Efimova, N., Efimov, A., & Kaverina, I. (2009) · Nature Cell Biology · doi:10.1038/ncb1920 · Cited by 294
Fass, E., Shvets, E., Degani, I., Hirschberg, K., & Elazar, Z. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607031200 · Cited by 286
Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B
Mann, S. S., & Hammarback, J. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78150-2 · Cited by 284
Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons
Hammond, J. W., Huang, C.-F., Kaech, S., Jacobson, C., Banker, G., & Verhey, K. J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0044 · Cited by 281
Differential turnover of tyrosinated and detyrosinated microtubules
Webster, D. R., Gundersen, G. G., Bulinski, J. C., & Borisy, G. G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.9040 · Cited by 261
The formin mDia2 stabilizes microtubules independently of its actin nucleation activity
Bartolini, F., Moseley, J. B., Schmoranzer, J., Cassimeris, L., Goode, B. L., & Gundersen, G. G. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709029 · Cited by 237
Multiple roles of the cytoskeleton in autophagy
Monastyrska, I., Rieter, E., Klionsky, D. J., & Reggiori, F. (2009) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/j.1469-185x.2009.00082.x · Cited by 234
Geeraert, C., Ratier, A., Pfisterer, S. G., Perdiz, D., Cantaloube, I., Rouault, A., Pattingre, S., Proikas‐Cezanne, T., Codogno, P., & Poüs, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.091553 · Cited by 222
Self-citationBim Inhibits Autophagy by Recruiting Beclin 1 to Microtubules
Luo, S., Garcı́a-Arencibia, M., Zhao, R., Puri, C., Toh, P. P. C., Sadiq, O., & Rubinsztein, D. C. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.040 · Cited by 209
Acetylated microtubules are required for fusion of autophagosomes with lysosomes
Xie, R., Nguyen, S., McKeehan, W. L., & Liu, L. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-89 · Cited by 195
Cytoskeletal elements are required for the formation and maturation of autophagic vacuoles
Aplin, A. E., Jasionowski, T., Tuttle, D. L., Lenk, S. E., & Dunn, W. A. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041520304 · Cited by 192
Webb, J. L., Ravikumar, B., & Rubinsztein, D. C. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.003 · Cited by 188
Cortical control of microtubule stability and polarization
Gundersen, G. G., Gomes, E. R., & Wen, Y. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.11.010 · Cited by 186
Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.
David-Pfeuty, T., Erickson, H., & Pantaloni, D. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5372 · Cited by 182
Involvement of microtubule motors in basolateral and apical transport in kidney cells
Lafont, F., Burkhardt, J. K., & Simons, K. (1994) · Nature · doi:10.1038/372801a0 · Cited by 181
Posttranslational Acetylation of α-Tubulin Constrains Protofilament Number in Native Microtubules
Cueva, J. G., Hsin, J., Huang, K. C., & Goodman, M. B. (2012) · Current Biology · doi:10.1016/j.cub.2012.05.012 · Cited by 178
From signaling pathways to microtubule dynamics: the key players
Etienne‐Manneville, S. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.008 · Cited by 171
Differential microtubule requirements for transcytosis in MDCK cells.
Hunziker, W., Mâle, P., & Mellman, I. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07560.x · Cited by 160
Topalidou, I., Keller, C., Kalebic, N., Nguyen, K. C. Q., Somhegyi, H., Politi, K. A., Heppenstall, P. A., Hall, D. H., & Chalfie, M. (2012) · Current Biology · doi:10.1016/j.cub.2012.03.066 · Cited by 159
UNC-51/ATG1 kinase regulates axonal transport by mediating motor–cargo assemblyPreprint
Toda, H., Mochizuki, H., Flores, R., Josowitz, R., Krasieva, T. B., LaMorte, V. J., Suzuki, E., Gindhart, J. G., Furukubo-Tokunaga, K., & Tomoda, T. (2008) · Genes & Development · doi:10.1101/gad.1734608 · Cited by 142
Lin, S. X. H., Gundersen, G. G., & Maxfield, F. R. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-05-0224 · Cited by 133
Detyrosinated (Glu) microtubules are stabilized by an ATP-sensitive plus-end cap
Infante, A. S., Stein, M. S., Zhai, Y., Borisy, G. G., & Gundersen, G. G. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.22.3907 · Cited by 127
Cardoso, C. M. P., Groth‐Pedersen, L., Høyer-Hansen, M. H., Kirkegaard, T., Corcelle, E., Andersen, J., Jäättelä, M., & Nylandsted, J. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004424 · Cited by 125
Xie, R., Nguyen, S., McKeehan, K. A., Wang, F., McKeehan, W. L., & Leyuan, L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.206532 · Cited by 124
Luminal Localization of α-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled Microtubules
Soppina, V., Herbstman, J. F., Skiniotis, G., & Verhey, K. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048204 · Cited by 116
Veldhoen, R. A., Banman, S. L., Hemmerling, D., Odsen, R., Simmen, T., Simmonds, A. J., Underhill, D. A., & Goping, I. S. (2012) · Oncogene · doi:10.1038/onc.2012.92 · Cited by 114
Amenta, J. S., Sargus, M. J., & Baccino, F. M. (1977) · Biochemical Journal · doi:10.1042/bj1680223 · Cited by 109
Kouno, T., Mizuguchi, M., Tanida, I., Ueno, T., Kanematsu, T., Mori, Y., Shinoda, H., Hirata, M., Kominami, E., & Kawano, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413565200 · Cited by 103
Push-me-pull-you: how microtubules organize the cell interior
Tolić, I. M. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0321-0 · Cited by 99
Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro
Walter, W. J., Beránek, V., Fischermeier, E., & Diez, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042218 · Cited by 97
Elastic and damping forces generated by confined arrays of dynamic microtubules
Howard, J. (2006) · Physical Biology · doi:10.1088/1478-3975/3/1/006 · Cited by 93
Kamath, K., Okouneva, T., Larson, G., Panda, D., Wilson, L., & Jordan, M. A. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0113 · Cited by 90
Arduíno, D. M., Esteves, A. R., Cortes, L., Silva, D. F., Patel, B., Grazina, M. M., Swerdlow, R. H., Oliveira, C. R., & Cardoso, S. M. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds309 · Cited by 87
Lorin, S., Borges, A., Santos, L. R. D., Souquère, S., Pierron, G., Ryan, K. M., Codogno, P., & Djavaheri‐Mergny, M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1270 · Cited by 82
Self-citationGuignot, J., Bernet‐Camard, M., Poüs, C., Plançon, L., Bouguénec, C. L., & Servin, A. L. (2001) · Infection and Immunity · doi:10.1128/iai.69.3.1856-1868.2001 · Cited by 78
Self-citationMizuno, M., & Singer, S. J. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.5.1321 · Cited by 65
Lysosome positioning coordinates mTORC1 activity and autophagy
Poüs, C., & Codogno, P. (2011) · Nature Cell Biology · doi:10.1038/ncb0411-342 · Cited by 61
Self-citationFunctional Specialization of Stable and Dynamic Microtubules in Protein Traffic in WIF-B Cells
Poüs, C., Chabin-Brion, K., Drechou, A., Barbot, L., Phung-Koskas, T., Settegrana, C., Bourguet‐Kondracki, M., Maurice, M., Cassio, D., Guyot, M., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.153 · Cited by 51
Self-citationMicrotubule depolymerization inhibits transport of cathepsin D from the Golgi apparatus to lysosomes
Scheel, J., Matteoni, R., Ludwig, T., Hoflack, B., & Kreis, T. E. (1990) · Journal of Cell Science · doi:10.1242/jcs.96.4.711 · Cited by 46
Joseph, R. A., Shepard, B. D., Kannarkat, G. T., Rutledge, T. W., Tuma, D. J., & Tuma, P. L. (2007) · Hepatology · doi:10.1002/hep.22014 · Cited by 40
New Targets for Acetylation in Autophagy
Hamaï, A., & Codogno, P. (2012) · Science Signaling · doi:10.1126/scisignal.2003187 · Cited by 36
Self-citationReunanen, H., Marttinen, M. T., & Hirsimäki, P. (1988) · Experimental and Molecular Pathology · doi:10.1016/0014-4800(88)90048-2 · Cited by 30
What is the advantage of a transient precursor in autophagosome biogenesis?
Ktistakis, N. T., Andrews, S., & Long, J. (2011) · Autophagy · doi:10.4161/auto.7.1.13697 · Cited by 18
Flagged first, then by citations
Cited by
Sorted by citations
The cell biology of the retinal pigment epithelium
Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422
“Post-translational modifications of tubulin such as acetylation and tyrosination/detyrosination can act either singly or in concert with other modifications to control motor recruitment in a cargo-specific manner (Hammond et al., 2008; Mackeh et al., 2013).”
BackgroundThe Cytoskeleton-Autophagy Connection
Kast, D. J., & Dominguez, R. (2017) · Current Biology · doi:10.1016/j.cub.2017.02.061 · Cited by 267
Mitophagy in Cancer: A Tale of Adaptation
Vara‐Pérez, M., Felipe‐Abrio, B., & Agostinis, P. (2019) · Cells · doi:10.3390/cells8050493 · Cited by 264
“autophagy (and mitophagy by extension) is highly sensitive to microtubule-dynamics modulators since microtubules are essential for the autophagosome fusion with the lysosome [295,296].”
BackgroundAutophagy regulation and its role in cancer
Lorin, S., Hamaï, A., Mehrpour, M., & Codogno, P. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.06.007 · Cited by 261
Self-citationPharmacologic agents targeting autophagy
Vakifahmetoglu-Norberg, H., Xia, H., & Yuan, J. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73937 · Cited by 247
“The destabilization of microtubules by either vinblastine (64), nocodazole, or cytochalasin B and D blocks the maturation of autophagosomes (65); conversely, taxol-mediated microtubule stabilization increases the fusion between autophagic vacuoles and lysosomes (66, 67).”
Metadata
- Authors
- Mackeh, R., Perdiz, D., Lorin, S., Codogno, P., & Poüs, C.
- Affiliations
- Université Paris-Sud (FR)
- Inserm (FR)
- Corresponding author
- Codogno, Patrice
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2013-03-01
- Volume
- 126
- Issue
- 5
- Pages
- 1071-1080
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2098921256
- Semantic Scholar
- bd987f4dde12826f66e2891ff2e65de145d37370
- Cited by
- 212
- References
- 110
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 13 · 2023: 13 · 2022: 20 · 2021: 20 · 2020: 20 · 2019: 21 · 2018: 17 · 2017: 20 · 2016: 16 · 2015: 10 · 2014: 18 · 2013: 3
- FWCI
- 11.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- autophagy, microtubules, autophagosome formation, autophagosome transport, autolysosomes, microtubule dynamics, tubulin post-translational modifications, microtubule motor proteins, nutrient deprivation, organelle degradation
- MeSH terms
- Animals, Autophagy, Humans, Lysosomes, Microtubules, Models, Biological, Phagocytosis, Protein Processing, Post-Translational, Tubulin
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review