The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
CD44 and β3 Integrin Organize Two Functionally Distinct Actin-based Domains in Osteoclasts
Open accessAbstract
The actin cytoskeleton of mature osteoclasts (OCs) adhering to nonmineralized substrates is organized in a belt of podosomes reminiscent of the sealing zone (SZ) found in bone resorbing OCs. In this study, we demonstrate that the belt is composed of two functionally different actin-based domains: podosome cores linked with CD44, which are involved in cell adhesion, and a diffuse cloud associated with β3 integrin, which is involved in cell adhesion and contraction. Wiskott Aldrich Syndrome Protein (WASp) Interacting Protein (WIP)−/− OCs were devoid of podosomes, but they still exhibited actin clouds. Indeed, WIP−/− OCs show diminished expression of WASp, which is required for podosome formation. CD44 is a novel marker of OC podosome cores and the first nonintegrin receptor detected in these structures. The importance of CD44 is revealed by showing that its clustering restores podosome cores and WASp expression in WIP−/− OCs. However, although CD44 signals are sufficient to form a SZ, the presence of WIP is indispensable for the formation of a fully functional SZ.
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
“It is important to mention that these domains are only formed when osteoclasts are in contact with extracellular mineralized matrix, in a process which α v β 3-integrin, as well as the CD44, mediates the attachment of the osteoclast podosomes to the bone surface [96–99].”
From Biology of Bone Tissue: Structure, Function, and Factors That Influence Bone Cells (2015) · cites this paper as [99]
Citations
Cites
Osteoclast differentiation and activation
Boyle, W. J., Simonet, W. S., & Lacey, D. L. (2003) · Nature · doi:10.1038/nature01658 · Cited by 6,670 · cited 4×
“Recombinant human RANK-L and human M-CSF were produced as described previously (Destaing et al., 2003).”
BackgroundInfluentialOsteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation.
Lacey, D. L., Timms, E., Tan, H.-L., Kelley, M. J., Dunstan, C. R., Burgess, T., Elliott, R., Colombero, A., Elliott, G., Scully, S., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81569-x · Cited by 5,439
CD44: From adhesion molecules to signalling regulators
Ponta, H., Sherman, L. S., & Herrlich, P. A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1004 · Cited by 2,458
Osteopontin--a possible anchor of osteoclasts to bone.
Reinholt, F. P., Hultenby, K. R., Oldberg, Å., & Heinegård, D. K. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4473 · Cited by 831
Mice lacking beta3 integrins are osteosclerotic because of dysfunctional osteoclasts.
McHugh, K. P., Hodivala-Dilke, K., Zheng, M., Namba, N., Lam, J. D., Novack, D., Feng, X., Ross, F., Hynes, R. O., & Teitelbaum, S. L. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8905 · Cited by 786
Goodison, S., Urquidi, V., & Tarin, D. (1999) · Molecular Pathology · doi:10.1136/mp.52.4.189 · Cited by 682
The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
Linder, S. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.01.002 · Cited by 640
Podosomes: adhesion hot-spots of invasive cells
Linder, S., & Aepfelbacher, M. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(03)00128-4 · Cited by 615
Destaing, O., Saltel, F., Géminard, J.-C., Jurdic, P., & Bard, F. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0389 · Cited by 547
Self-citationTranscellular Diapedesis Is Initiated by Invasive Podosomes
Carman, C. V., Sage, P. T., Sciuto, T. E., de la Fuente, M. Á., Geha, R. S., Ochs, H. D., Dvorak, H. F., Dvořàk, A. M., & Springer, T. A. (2007) · Immunity · doi:10.1016/j.immuni.2007.04.015 · Cited by 497
Research works printed but not linked: 2
- Linder S., 2007, Trends Cell Biol, 17, 107, 10.1016/j.tcb.2007.01.002 · DOI
- Mizutani K., 2002, Cancer Res, 62, 669
Cited by
Sorted by citations
Biology of Bone Tissue: Structure, Function, and Factors That Influence Bone Cells
Florencio-Silva, R., Sasso, G. R. D. S., Sasso-Cerri, E., Simões, M. J., & Cerri, P. S. (2015) · BioMed Research International · doi:10.1155/2015/421746 · Cited by 2,044
Rasmussen, M. K., Mestre, H., & Nedergaard, M. (2021) · Physiological Reviews · doi:10.1152/physrev.00031.2020 · Cited by 642
Matrix Metalloproteinases Shape the Tumor Microenvironment in Cancer Progression
Niland, S., Riscanevo, A. X., & Eble, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010146 · Cited by 546
Crockett, J. C., Rogers, M. J., Coxon, F. P., Hocking, L. J., & Helfrich, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.063032 · Cited by 532
Assembly and biological role of podosomes and invadopodia
Gimona, M., Buccione, R., Courtneidge, S. A., & Linder, S. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.01.005 · Cited by 404
Degrading Devices: Invadosomes in Proteolytic Cell Invasion
Linder, S., Wiesner, C., & Himmel, M. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154216 · Cited by 392
Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
Albigès‐Rizo, C., Destaing, O., Fourcade, B., Planus, E., & Block, M. R. (2009) · Journal of Cell Science · doi:10.1242/jcs.052704 · Cited by 328
Actin assembly mechanisms at a glance
Rottner, K., Faix, J., Bogdan, S., Linder, S., & Kerkhoff, E. (2017) · Journal of Cell Science · doi:10.1242/jcs.206433 · Cited by 298
Osteoclast lineage and function
Väänänen, H. K., & Laitala‐Leinonen, T. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.03.037 · Cited by 274
Invadopodia: At the cutting edge of tumour invasion
Stylli, S. S., Kaye, A. H., & Lock, P. (2008) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2008.03.003 · Cited by 226
Labernadie, A., Bouissou, A., Delobelle, P., Balor, S., Voituriez, R., Proag, A., Fourquaux, I., Thibault, C., Christophe Vieu, A., Poincloux, R., et al. (2014) · Nature Communications · doi:10.1038/ncomms6343 · Cited by 203
Regenerative potential of glycosaminoglycans for skin and bone
Salbach‐Hirsch, J., Rachner, T. D., Rauner, M., Hempel, U., Anderegg, U., Franz, S., Simon, J., & Hofbauer, L. C. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0843-2 · Cited by 208
Mechanisms and roles of podosomes and invadopodia
Linder, S., Cervero, P., Eddy, R. J., & Condeelis, J. S. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00530-6 · Cited by 185
Podosome organization drives osteoclast-mediated bone resorption
Georgess, D., Machuca‐Gayet, I., Blangy, A., & Jurdic, P. (2014) · Cell Adhesion & Migration · doi:10.4161/cam.27840 · Cited by 181
Self-citationSaltel, F., Mortier, E., Hytönen, V. P., Jacquier, M., Zimmermann, P., Viola Vogel, B., Liu, W., & Wehrle‐Haller, B. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200908134 · Cited by 181
Self-citationLinder, S. (2009) · Journal of Cell Science · doi:10.1242/jcs.032631 · Cited by 174
Saltel, F., Chabadel, A., Bonnelye, E., & Jurdic, P. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.01.001 · Cited by 170
Self-citationSchmidt, S., Nakchbandi, I. A., Ruppert, R., Kawelke, N., Hess, M. W., Pfaller, K., Jurdic, P., Fässler, R., & Moser, M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201007141 · Cited by 169
Self-citationPodosome-type adhesions and focal adhesions, so alike yet so different
Block, M. R., Badowski, C., Millon‐Frémillon, A., Bouvard, D., Bouin, A., Faurobert, E., Gerber, D., Planus, E., & Albigès‐Rizo, C. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.02.012 · Cited by 165
Terkawi, M. A., Matsumae, G., Shimizu, T., Takahashi, D., Kadoya, K., & Iwasaki, N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031786 · Cited by 174
The regulation of osteoclast function and bone resorption by small GTPases
Itzstein, C., Coxon, F. P., & Rogers, M. J. (2011) · Small GTPases · doi:10.4161/sgtp.2.3.16453 · Cited by 160
Wiesner, C., Faix, J., Himmel, M., Bentzien, F., & Linder, S. (2010) · Blood · doi:10.1182/blood-2009-12-257089 · Cited by 151
Gawden‐Bone, C. M., Zhou, Z., King, E. M. J., Prescott, A. R., Watts, C. K. W., & Lucocq, J. M. (2010) · Journal of Cell Science · doi:10.1242/jcs.056515 · Cited by 144
Invadosome regulation by adhesion signaling
Destaing, O., Block, M. R., Planus, E., & Albigès‐Rizo, C. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.04.002 · Cited by 149
Rho GTPases in osteoclasts: Orchestrators of podosome arrangement
Ory, S., Brazier, H., Pawlak, G., & Blangy, A. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.03.002 · Cited by 133
Goethem, E. V., Guiet, R., Balor, S., Charrière, G. M., Poincloux, R., Labrousse, A. M., Maridonneau‐Parini, I., & Cabec, V. L. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.07.011 · Cited by 131
The Sealing Zone in Osteoclasts: A Self-Organized Structure on the Bone
Takito, J., Inoue, S., & Nakamura, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19040984 · Cited by 122
Osteoclast fusion and regulation by RANKL-dependent and independent factors
Xing, L. (2012) · World Journal of Orthopedics · doi:10.5312/wjo.v3.i12.212 · Cited by 122
Mellis, D. J., Itzstein, C., Helfrich, M., & Crockett, J. C. (2011) · Journal of Endocrinology · doi:10.1530/joe-11-0212 · Cited by 117
Podosomes in adhesion, migration, mechanosensing and matrix remodeling
Schachtner, H., Calaminus, S. D. J., Thomas, S. G., & Machesky, L. M. (2013) · Cytoskeleton · doi:10.1002/cm.21119 · Cited by 119
Juin, A., Billottet, C., Moreau, V., Destaing, O., Albigès‐Rizo, C., Rosenbaum, J., Genot, E. M., & Saltel, F. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-07-0594 · Cited by 111
Self-citationTools of the trade: podosomes as multipurpose organelles of monocytic cells
Linder, S., & Wiesner, C. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1731-z · Cited by 106
Invadosomes: Intriguing structures with promise
Saltel, F., Daubon, T., Juin, A., Ganuza, I. E., Veillat, V., & Genot, E. M. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.05.011 · Cited by 98
Self-citationOsteoclast motility: Putting the brakes on bone resorption
Novack, D. V., & Faccio, R. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.09.005 · Cited by 93
Modulation of osteoclast differentiation and bone resorption by Rho GTPases
Touaitahuata, H., Blangy, A., & Vives, V. (2014) · Small GTPases · doi:10.4161/sgtp.28119 · Cited by 93
Probing the mechanical landscape – new insights into podosome architecture and mechanics
van den Dries, K., Linder, S., Maridonneau‐Parini, I., & Poincloux, R. (2019) · Journal of Cell Science · doi:10.1242/jcs.236828 · Cited by 92
Macrophage Mesenchymal Migration Requires Podosome Stabilization by Filamin A
Guiet, R., Vérollet, C., Lamsoul, I., Cougoule, C., Poincloux, R., Labrousse, A. M., Calderwood, D., Glogauer, M., Lutz, P. G., & Maridonneau‐Parini, I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.307124 · Cited by 85
pH regulators in invadosomal functioning: Proton delivery for matrix tasting
Brisson, L., Reshkin, S. J., Goré, J., & Roger, S. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.04.004 · Cited by 88
Supervillin Reorganizes the Actin Cytoskeleton and Increases Invadopodial Efficiency
Crowley, J. L., Smith, T. C., Fang, Z., Takizawa, N., & Luna, E. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0867 · Cited by 78
Feel the force: Podosomes in mechanosensing
Linder, S., & Wiesner, C. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.11.026 · Cited by 82
The microenvironment controls invadosome plasticity
Martino, J. S. D., Henriet, E., Ezzoukhry, Z., Goetz, J. G., Moreau, V., & Saltel, F. (2016) · Journal of Cell Science · doi:10.1242/jcs.182329 · Cited by 76
Self-citationThe CD44s splice isoform is a central mediator for invadopodia activity
Zhao, P., Xu, Y., Wei, Y., Qiu, Q., Chew, T., Kang, Y., & Cheng, C. (2016) · Journal of Cell Science · doi:10.1242/jcs.171959 · Cited by 75
PGC1β Organizes the Osteoclast Cytoskeleton by Mitochondrial Biogenesis and Activation
Zhang, Y., Rohatgi, N., Novack, D. V., Schilling, J. D., Teitelbaum, S. L., & Zou, W. (2018) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3398 · Cited by 72
Cervero, P., Himmel, M., Krüger, M., & Linder, S. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.05.005 · Cited by 75
The kinesin KIF9 and reggie/flotillin proteins regulate matrix degradation by macrophage podosomes
Cornfine, S., Himmel, M., Kopp, P., Azzouzi, K. E., Wiesner, C., Krüger, M., Rudel, T., & Linder, S. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-05-0394 · Cited by 68
A Complex and Evolutive Character: Two Face Aspects of ECM in Tumor Progression
Sala, M., Ros, M., & Saltel, F. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01620 · Cited by 67
Self-citationMetalloproteinase MT1-MMP islets act as memory devices for podosome reemergence
Azzouzi, K. E., Wiesner, C., & Linder, S. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201510043 · Cited by 63
The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes
Panzer, L., Trübe, L., Klose, M., Joosten, B., Slotman, J. A., Cambi, A., & Linder, S. (2015) · Journal of Cell Science · doi:10.1242/jcs.177691 · Cited by 63
Cervero, P., Wiesner, C., Bouissou, A., Poincloux, R., & Linder, S. (2018) · Nature Communications · doi:10.1038/s41467-018-02904-x · Cited by 59
Importance of RhoGTPases in formation, characteristics, and functions of invadosomes
Spuul, P., Ciufici, P., Veillat, V., Leclercq, A., Daubon, T., Kramer, I. M., & Genot, E. M. (2014) · Small GTPases · doi:10.4161/sgtp.28713 · Cited by 57
Self-citationChen, Z.-H., Wu, J., Guo, D., Li, Y., Chen, M.-N., Zhang, Z., Yuan, Z.-D., Zhang, K., Chen, W., Fan, T., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101842 · Cited by 56
Michopoulou, A., Montmasson, M., Garnier, C., Lambert, E., Dayan, G., & Rousselle, P. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.06.004 · Cited by 53
Podosomes: Multipurpose organelles?
Veillat, V., Spuul, P., Daubon, T., Egaña, I., Kramer, I. M., & Genot, E. M. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.05.020 · Cited by 58
Self-citationMartino, J. S. D., Paysan, L., Gest, C., Lagrée, V., Juin, A., Saltel, F., & Moreau, V. (2014) · Cell Adhesion & Migration · doi:10.4161/cam.28833 · Cited by 50
Self-citationWIP: WASP-interacting proteins at invadopodia and podosomes
García, E., Jones, G. E., Machesky, L. M., & Antón, I. M. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.06.002 · Cited by 54
Self-citationWASP and WIP regulate podosomes in migrating leukocytes
Calle, Y., Antón, I. M., Thrasher, A. J., & Jones, G. E. (2008) · Journal of Microscopy · doi:10.1111/j.1365-2818.2008.02062.x · Cited by 50
Self-citationChapter 1 Roles of Caldesmon in Cell Motility and Actin Cytoskeleton Remodeling
Lin, J. J., Li, Y., Eppinga, R., Wang, Q., & Jin, J. (2009) · International review of cytology · doi:10.1016/s1937-6448(08)02001-7 · Cited by 49
Georgess, D., Mazzorana, M., Terrado, J., Delprat, C., Chamot, C., Guasch, R. M., Pérez‐Roger, I., Jurdic, P., & Machuca‐Gayet, I. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0363 · Cited by 46
Self-citationOsteoactivin inhibition of osteoclastogenesis is mediated through CD44-ERK signaling
Sondag, G. R., Mbimba, T., Moussa, F. M., Novak, K. M., Yu, B., Jaber, F. A., Abdelmagid, S. M., Geldenhuys, W. J., & Safadi, F. F. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.78 · Cited by 48
Integral roles of a guanine nucleotide exchange factor, FARP2, in osteoclast podosome rearrangements
Takegahara, N., Kang, S., Nojima, S., Takamatsu, H., Okuno, T., Kikutani, H., Toyofuku, T., & Kumanogoh, A. (2010) · The FASEB Journal · doi:10.1096/fj.10-158212 · Cited by 47
Antelmi, E., Cardone, R. A., Greco, M. R., Rubino, R., Sole, F. D., Martino, N. A., Casavola, V., Carcangiu, M.-L., Moro, L., & Reshkin, S. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075113 · Cited by 42
Integrins: Moonlighting Proteins in Invadosome Formation
Peláez, R., Pariente, A., Pérez-Sala, Á., & Larráyoz, I. M. (2019) · Cancers · doi:10.3390/cancers11050615 · Cited by 44
Madel, M., Ibáñez, L., Rouleau, M., Wakkach, A., & Blin‐Wakkach, C. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02567 · Cited by 41
Dufrançais, O., Mascarau, R., Poincloux, R., Maridonneau‐Parini, I., Raynaud‐Messina, B., & Vérollet, C. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03875-x · Cited by 40
Effects of Isoform-selective Phosphatidylinositol 3-Kinase Inhibitors on Osteoclasts
Shugg, R. P. P., Thomson, A., Tanabe, N., Kashishian, A., Steiner, B. H., Puri, K. D., Pereverzev, A., Lannutti, B. J., Jirik, F. R., Dixon, S. J., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.507525 · Cited by 38
Gawden‐Bone, C. M., West, M. A., Morrison, V. L., Edgar, A. J., McMillan, S. J., Dill, B. D., Trost, M., Prescott, A. R., Fagerholm, S. C., & Watts, C. K. W. (2014) · Journal of Cell Science · doi:10.1242/jcs.151167 · Cited by 38
Bañón‐Rodríguez, I., Monypenny, J., Ragazzini, C., Franco, A. C. G., Calle, Y., Jones, G. E., & Antón, I. M. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.09.001 · Cited by 43
Self-citationCofilin Activation during Podosome Belt Formation in Osteoclasts
Blangy, A., Touaitahuata, H., Crès, G., & Pawlak, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045909 · Cited by 37
Myosins in Osteoclast Formation and Function
Lee, B. S. (2018) · Biomolecules · doi:10.3390/biom8040157 · Cited by 33
The osteoclast, a target cell for microorganisms
Raynaud‐Messina, B., Vérollet, C., & Maridonneau‐Parini, I. (2019) · Bone · doi:10.1016/j.bone.2019.06.023 · Cited by 34
Hazama, R., Qu, X., Kunio, Y., Tanaka, C., Kinoshita, E., He, J., Takahashi, S., Tohyama, K., Yamamura, H., & Tohyama, Y. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01317.x · Cited by 32
Signaling networks regulating leukocyte podosome dynamics and function
Dovas, A., & Cox, D. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.02.004 · Cited by 34
Bonnelye, E., Saltel, F., Chabadel, A., Zirngibl, R. A., Aubin, J. E., & Jurdic, P. (2010) · Journal of Molecular Endocrinology · doi:10.1677/jme-10-0024 · Cited by 32
Self-citationEllis, S. J., Lostchuck, E., Goult, B. T., Bouaouina, M., Fairchild, M. J., López-Ceballos, P., Calderwood, D., & Tanentzapf, G. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004756 · Cited by 30
New Insights into Adhesion Signaling in Bone Formation
Brunner, M., Jurdic, P., Tuckerman, J., Block, M. R., & Bouvard, D. (2013) · International review of cytology · doi:10.1016/b978-0-12-407695-2.00001-9 · Cited by 30
Self-citationXiang, B., Liu, Y., Zhao, W., Zhao, H., & Yu, H. (2018) · Cell Biology International · doi:10.1002/cbin.11033 · Cited by 28
Zur, Y., Rosenfeld, L., Keshelman, C. A., Dalal, N., Ram, G. G., Orenbuch, A., Einav, Y., Levaot, N., & Papo, N. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2002979 · Cited by 27
Abl-mediated PI3K activation regulates macrophage podosome formation
Zhou, Y., Feng, Z., Cao, F., Liu, X., Xia, X., & Yu, C. (2020) · Journal of Cell Science · doi:10.1242/jcs.234385 · Cited by 26
Growth factor-triggered de-sialylation controls glycolipid-lectin-driven endocytosis
MacDonald, E., Forrester, A. R., Valades‐Cruz, C. A., Madsen, T. D., Hetmanski, J. H. R., Dransart, E., Ng, Y., Godbole, R. K., Ananthan, A. S., Leconte, L., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01616-x · Cited by 25
Bone cell–matrix protein interactions
Marie, P. J. (2009) · Osteoporosis International · doi:10.1007/s00198-009-0856-7 · Cited by 25
The circle of life: Phases of podosome formation, turnover and reemergence
Weber, K., Hey, S., Cervero, P., & Linder, S. (2022) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2022.151218 · Cited by 24
Na, W., Lee, E., Kang, M., Kim, Y., Kim, D. Y., Oh, H., Kim, S., Oh, S. Y., & Kang, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228581 · Cited by 24
Tyrosine phosphorylation of WIP releases bound WASP and impairs podosome assembly in macrophages
Vijayakumar, V., Monypenny, J., Chen, X. J., Machesky, L. M., Lilla, S., Thrasher, A. J., Anton, I. M., Calle, Y., & Jones, G. E. (2014) · Journal of Cell Science · doi:10.1242/jcs.154880 · Cited by 21
Self-citationSuarez, J. S., Main, H. G., Muralidhar, G. G., Elfituri, O., Xu, H., Kajdacsy‐Balla, A., & Barbolina, M. V. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-1205 · Cited by 21
Osteoclast Biology: Regulation of Formation and Function
Choi, Y., Faccio, R., Teitelbaum, S. L., & Takayanagi, H. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800571-2.00004-9 · Cited by 21
The podosome cap: past, present, perspective
Linder, S., & Cervero, P. (2020) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2020.151087 · Cited by 21
Podosome regulation by Rho GTPases in myeloid cells
van Helden, S. F. G., & Hordijk, P. L. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.05.008 · Cited by 20
The phytochemical plumbagin reciprocally modulates osteoblasts and osteoclasts
Yadav, A. M., Bagade, M. M., Ghumnani, S., Raman, S., Saha, B., Kubatzky, K. F., & Ashma, R. (2021) · Biological Chemistry · doi:10.1515/hsz-2021-0290 · Cited by 20
Nanoscale architecture and coordination of actin cores within the sealing zone of human osteoclasts
Portes, M., Mangeat, T., Escallier, N., Dufrançais, O., Raynaud‐Messina, B., Thibault, C., Maridonneau‐Parini, I., Vérollet, C., & Poincloux, R. (2022) · eLife · doi:10.7554/elife.75610 · Cited by 21
Spatiotemporal coordination of actin regulators generates invasive protrusions in cell–cell fusion
Lu, Y., Walji, T. A., Ravaux, B., Pandey, P., Yang, C., Li, B., Luvsanjav, D., Lam, K. H., Zhang, R., Luo, Z., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01541-5 · Cited by 18
Invadosomes ndash shaping actin networks to follow mechanical cues
Innocenti, M. (2016) · Frontiers in bioscience · doi:10.2741/4444 · Cited by 18
Rau, L.-R., Tsao, S.-W., Liaw, J., & Tsai, S. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.6b00386 · Cited by 17
Sharma, A., Sharma, L. K., & Goyal, R. (2020) · Current Drug Targets · doi:10.2174/1389450121666200910160404 · Cited by 33
Takito, J., & Nakamura, M. (2012) · Communicative & Integrative Biology · doi:10.4161/cib.20980 · Cited by 17
Podosomes are dispensable for osteoclast differentiation and migration
Touaitahuata, H., Planus, E., Albigès‐Rizo, C., Blangy, A., & Pawlak, G. (2013) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2013.03.001 · Cited by 17
Zhao, H., Liu, X., Zou, H., Dai, N., Yao, L., Zhang, X., Gao, Q., Liu, W. X., Gu, J., Yuan, Y., et al. (2016) · Cell Adhesion & Migration · doi:10.1080/19336918.2015.1129480 · Cited by 16
Pan, Y., Tseng, W.-S., Chang, P.-W., & Chen, H. (2013) · Journal of Cell Science · doi:10.1242/jcs.134361 · Cited by 17
Luo, T., Liu, H., Feng, W., Liu, D., Du, J., Sun, J., Wang, W., Han, X., Guo, J., Amizuka, N., et al. (2016) · Cell Proliferation · doi:10.1111/cpr.12317 · Cited by 15
Integrin linked kinase (ILK) regulates podosome maturation and stability in dendritic cells
Griera, M., Martín-Villar, E., Bañón‐Rodríguez, I., Blundell, M. P., Jones, G. E., Anton, I. M., Thrasher, A. J., Rodrı́guez-Puyol, M., & Calle, Y. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.01.021 · Cited by 14
Self-citationMira‐Pascual, L., Tran, A. N., Andersson, G., Näreoja, T., & Lång, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020538 · Cited by 14
Metadata
- Authors
- Chabadel, A., Bañon-Rodríguez, I., Cluet, D., Rudkin, B. B., Wehrle-Haller, B., Genot, E., Jurdic, P., Anton, I. M., & Saltel, F.
- Affiliations
- Lyon 1 Université (FR)
- Centro de Biología Molecular “Severo Ochoa,” Consejo Superior de Investigaciones Cientificas-Universidad Autonoma de Madrid, 28049 Madrid, Spain;
- Department of Cellular Physiology and Metabolism, Centre Médical Universitaire, 1211 Geneva 4, Switzerland; and
- Inserm (FR)
- Consejo Superior de Investigaciones Científicas (ES)
- Venue
- Molecular Biology of the Cell
- Published
- 2007-12
- Volume
- 18
- Issue
- 12
- Pages
- 4899-4910
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC2096584
- OpenAlex
- W2160358447
- Cited by
- 154
- References
- 57
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 4 · 2023: 6 · 2022: 9 · 2021: 6 · 2020: 13 · 2019: 10 · 2018: 9 · 2017: 3 · 2016: 8 · 2015: 8 · 2014: 11 · 2013: 7 · 2012: 11
- FWCI
- 4.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- HAL (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- European Social Fund
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bone Metabolism and Diseases
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- osteoclasts, CD44, CD61, actin cytoskeleton, podosomes, sealing zone, WIP, wasps, cell adhesion, bone resorption, receptor clustering
- MeSH terms
- Actins, Animals, Bone Resorption, Intracellular Membranes, Osteoclasts, Signal Transduction, Mice, Knockout, Hyaluronan Receptors, Integrin beta3, Wiskott-Aldrich Syndrome Protein, Mice
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