Kindlins: essential regulators of integrin signalling and cell-matrix adhesion
Open accessAbstract
Integrin-mediated cell-ECM (extracellular matrix) adhesion is a fundamental process that controls cell behaviour. For correct cell-ECM adhesion, both the ligand-binding affinity and the spatial organization of integrins must be precisely controlled; how integrins are regulated, however, is not completely understood. Kindlins constitute a family of evolutionarily conserved cytoplasmic components of cell-ECM adhesions that bind to beta-integrin cytoplasmic tails directly and cooperate with talin in integrin activation. In addition, kindlins interact with many components of cell-ECM adhesions--such as migfilin and integrin-linked kinase--to promote cytoskeletal reorganization. Loss of kindlins causes severe defects in integrin signalling, cell-ECM adhesion and cytoskeletal organization, resulting in early embryonic lethality (kindlin-2), postnatal lethality (kindlin-3) and Kindler syndrome (kindlin-1). It is therefore clear that kindlins, together with several other integrin-proximal proteins, are essential for integrin signalling and cell-ECM adhesion regulation.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
FERMT1 directly binds the cytoplasmic tail of β1 integrin to enable signaling and mediate cell spreading.
“FERMT1 (also known as kindlin-1) directly binds the cytoplasmic tail of β1 integrin to enable signaling and mediate cell spreading and controls murine cutaneous stem cell homeostasis (Kloeker et al., 2004, Larjava et al., 2008, Rognoni et al., 2014).”
From Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020) · cites this paper as Larjava et al., 2008
FERMT1 controls murine cutaneous stem cell homeostasis.
“FERMT1 (also known as kindlin-1) directly binds the cytoplasmic tail of β1 integrin to enable signaling and mediate cell spreading and controls murine cutaneous stem cell homeostasis (Kloeker et al., 2004, Larjava et al., 2008, Rognoni et al., 2014).”
From Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020) · cites this paper as Larjava et al., 2008
The Introduction reports kindlin-1 expression in murine skin and effects of kindlin-1 deficiency on cultured keratinocytes, but neither establishes control of murine cutaneous stem cell homeostasis. Searches for “stem cell homeostasis,” “cutaneous stem cells,” and “stem cells” found no passage addressing that claim. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606 · see citing works
Talin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation
Tadokoro, S., Shattil, S. J., Eto, K., Tai, V., Liddington, R., de Pereda, J. M., Ginsberg, M. H., & Calderwood, D. (2003) · Science · doi:10.1126/science.1086652 · Cited by 1,211 · see citing works
Ramirez, A., Fisher, G., George, E. L., Sanning, E., Forouzani, M., Allen, J., Bak, R., Halley, W., Wheeler, G., her, et al. (2003) · Cited by 960 · see citing works
Bidirectional Transmembrane Signaling by Cytoplasmic Domain Separation in Integrins
Kim, M., Carman, C. V., & Springer, T. A. (2003) · Science · doi:10.1126/science.1084174 · Cited by 786 · see citing works
Calderwood, D. A., Zent, R., Grant, R., Rees, D. J. G., Hynes, R. O., & Ginsberg, M. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28071 · Cited by 720 · see citing works
Kindlin-3 is essential for integrin activation and platelet aggregation
Moser, M., Nieswandt, B., Ussar, S., Požgajová, M., & Fässler, R. (2008) · Nature Medicine · doi:10.1038/nm1722 · Cited by 700 · see citing works
Krüger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fässler, R., & Mann, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.033 · Cited by 680 · see citing works
Structural Basis of Integrin Activation by Talin
Wegener, K. L., Partridge, A. W., Han, J., Pickford, A. R., Liddington, R., Ginsberg, M. H., & Campbell, I. D. (2007) · Cell · doi:10.1016/j.cell.2006.10.048 · Cited by 677 · see citing works
Pearson, M. A., Reczek, D., Bretscher, A. P., & Karplus, P. A. (2000) · Cell · doi:10.1016/s0092-8674(00)80836-3 · Cited by 604 · see citing works
Hughes, P. E., Díaz‐González, F., Leong, L., Wu, C., McDonald, J. A., Shattil, S. J., & Ginsberg, M. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6571 · Cited by 571 · see citing works
Self-citationVinogradova, O., Vėlyvis, A., Velyviene, A., Hu, B., Haas, T. A., Plow, E. F., & Qin, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00906-6 · Cited by 529 · see citing works
Self-citationStructural Determinants of Integrin Recognition by Talin
García‐Álvarez, B., de Pereda, J. M., Calderwood, D., Ulmer, T. S., Critchley, D. R., Campbell, I. D., Ginsberg, M. H., & Liddington, R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00823-7 · Cited by 519 · see citing works
Kindlin-2 controls bidirectional signaling of integrinsPreprint
Montañez, E., Ussar, S., Schifferer, M., Bösl, M. R., Zent, R., Moser, M., & Fässler, R. (2008) · Genes & Development · doi:10.1101/gad.469408 · Cited by 452 · see citing works
Reconstructing and Deconstructing Agonist-Induced Activation of Integrin αIIbβ3
Han, J., Lim, C. J., Watanabe, N., Soriani, A., Ratnikov, B. I., Calderwood, D., Puzon-McLaughlin, W., Lafuente, E. M., Boussiotis, V. A., Shattil, S. J., et al. (2006) · Current Biology · doi:10.1016/j.cub.2006.08.035 · Cited by 447 · see citing works
The Phosphotyrosine Binding-like Domain of Talin Activates Integrins
Calderwood, D., Yan, B., de Pereda, J. M., García‐Álvarez, B., Fujioka, Y., Liddington, R., & Ginsberg, M. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111996200 · Cited by 412 · see citing works
Tu, Y., Wu, S., Shi, X., Chen, K., & Wu, C. (2003) · Cell · doi:10.1016/s0092-8674(03)00163-6 · Cited by 375 · see citing works
Self-citationKindlin-2 (Mig-2): a co-activator of β3 integrins
Ma, Y., Qin, J., Wu, C., & Plow, E. F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200710196 · Cited by 352 · see citing works
Self-citationSiegel, D. H., Ashton, G. H. S., Penagos, H., Lee, J. V., Feiler, H. S., Wilhelmsen, K. C., South, A. P., Smith, F. J. D., Prescott, A. R., Wessagowit, V., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/376609 · Cited by 346 · see citing works
Talin is required for integrin-mediated platelet function in hemostasis and thrombosis
Petrich, B. G., Marchese, P., Ruggeri, Z. M., Spiess, S., Weichert, R. A. M., Ye, F., Tiedt, R., Skoda, R. C., Monkley, S. J., Critchley, D. R., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071800 · Cited by 309 · see citing works
C. elegans PAT-4/ILK Functions as an Adaptor Protein within Integrin Adhesion Complexes
Mackinnon, A. C., Qadota, H., Norman, K. R., Moerman, D. G., & Williams, B. D. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00810-2 · Cited by 309 · see citing works
Nieswandt, B., Moser, M., Pleines, I., Varga-Szabó, D., Monkley, S., Critchley, D. R., & Fässler, R. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071827 · Cited by 273 · see citing works
Jobard, F. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg097 · Cited by 258 · see citing works
The Kindlins: Subcellular localization and expression during murine development
Ussar, S., Wang, H., Linder, S., Fässler, R., & Moser, M. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.06.030 · Cited by 255 · see citing works
Chen, Y. P., Djaffar, I., Pidard, D., Steiner, B., Cieutat, A.-M., Caen, J., & Rosa, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10169 · Cited by 221 · see citing works
CONGENITAL POIKILODERMA WITH TRAUMATIC BULLA FOKMATION AND PROGRESSIVE CUTANEOUS ATROPHY.
Kindler, T. (1954) · British Journal of Dermatology · doi:10.1111/j.1365-2133.1954.tb12598.x · Cited by 207 · see citing works
Critchley, D. R., & Gingras, A. R. (2008) · Journal of Cell Science · doi:10.1242/jcs.018085 · Cited by 206 · see citing works
Rogalski, T. M., Mullen, G. P., Gilbert, M., Williams, B. D., & Moerman, D. G. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.1.253 · Cited by 195 · see citing works
Integrin Bidirectional Signaling: A Molecular View
Qin, J., Vinogradova, O., & Plow, E. F. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020169 · Cited by 189 · see citing works
Self-citationThe MIG-2/Integrin Interaction Strengthens Cell-Matrix Adhesion and Modulates Cell Motility
Shi, X., Ma, Y., Tu, Y., Chen, K., Wu, S., Fukuda, K., Qin, J., Plow, E. F., & Wu, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611680200 · Cited by 182 · see citing works
Self-citationKloeker, S., Major, M. B., Calderwood, D. A., Ginsberg, M. H., Jones, D. A., & Beckerle, M. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307978200 · Cited by 163 · see citing works
Dowling, J. J., Gibbs, E. M., Russell, M. W. W., Goldman, D. J., Minarcik, J. C., Golden, J. A., & Feldman, E. L. (2008) · Circulation Research · doi:10.1161/circresaha.107.161489 · Cited by 161 · see citing works
The PINCH–ILK–parvin complexes: assembly, functions and regulation
Wu, C. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.01.006 · Cited by 149 · see citing works
Self-citationHerz, C., Aumailley, M., Schulte, C., Schlötzer-Schrehardt, U. M., Bruckner‐Tuderman, L., & Has, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606259200 · Cited by 145 · see citing works
Chen, Y., O'Toole, T., Ylänne, J., Rosa, J., & Ginsberg, M. (1994) · Blood · doi:10.1182/blood.v84.6.1857.bloodjournal8461857 · Cited by 125 · see citing works
Petrich, B. G., Fogelstrand, P., Partridge, A. W., Yousefi, N., Ablooglu, A. J., Shattil, S. J., & Ginsberg, M. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31024 · Cited by 119 · see citing works
Lai-Cheong, J. E., Ussar, S., Arita, K., Hart, I. R., & McGrath, J. A. (2008) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.58 · Cited by 94 · see citing works
Chronic colitis due to an epithelial barrier defect: the role of kindlin‐1 isoforms
Kern, J. S., Herz, C., Haan, E., Moore, D., Nottelmann, S., von Lilien, T., Greiner, P., Schmitt-Graeff, A. H., OPITZ, O. G., Bruckner‐Tuderman, L., et al. (2007) · The Journal of Pathology · doi:10.1002/path.2253 · Cited by 91 · see citing works
Migfilin and its binding partners: from cell biology to human diseases
Wu, C. (2005) · Journal of Cell Science · doi:10.1242/jcs.01639 · Cited by 84 · see citing works
Self-citationWeinstein, E. J., Bourner, M. J., Head, R., Zakeri, H., Bauer, C., & Mazzarella, R. A. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(03)00035-8 · Cited by 80 · see citing works
The Cytoplasmic Domain of αIIbβ3
Haas, T. A., & Plow, E. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6017 · Cited by 76 · see citing works
Self-citationRegulation of Integrin αIIbβ3 Activation by Distinct Regions of Its Cytoplasmic Tails
Ma, Y., Yang, J., Pesho, M. M., Vinogradova, O., Qin, J., & Plow, E. F. (2006) · Biochemistry · doi:10.1021/bi060279h · Cited by 70 · see citing works
Self-citationZhang, Y., Tu, Y., Gkretsi, V., & Wu, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512107200 · Cited by 68 · see citing works
Self-citationShimizu, H. (1997) · Archives of Dermatology · doi:10.1001/archderm.1997.03890450057007 · Cited by 64 · see citing works
Kindler Syndrome and Periodontal Disease: Review of the Literature and a 12‐Year Follow‐Up Case
Wiebe, C. B., Petricca, G., Häkkinen, L., Jiang, G., Wu, C., & Larjava, H. (2008) · Journal of Periodontology · doi:10.1902/jop.2008.070167 · Cited by 63 · see citing works
Self-citationA Suppressive Role of Mitogen Inducible Gene-2 in Mesenchymal Cancer Cell Invasion
Shi, X., & Wu, C. (2008) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-2026 · Cited by 47 · see citing works
Self-citationGenetic, biochemical and structural approaches to talin function
Critchley, D. R. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051308 · Cited by 45 · see citing works
Genetic, biochemical and structural approaches to talin function
Critchley, D. R. (2005) · Biochemical Society Transactions · doi:10.1042/bst0331308 · Cited by 38 · see citing works
Abnormal deposition of type VII collagen in Kindler syndrome
Wiebe, C. B., & Larjava, H. (1999) · Archives of Dermatological Research · doi:10.1007/s004030050377 · Cited by 32 · see citing works
Self-citationIntegrin activation—the importance of a positive feedback
Iber, D., & Campbell, I. D. (2006) · Bulletin of Mathematical Biology · doi:10.1007/s11538-005-9049-5 · Cited by 20 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Barczyk, M., Carracedo, S., & Gullberg, D. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0834-6 · Cited by 1,512 · see citing works
Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma
Ji, A. L., Rubin, A. J., Thrane, K., Jiang, S., Reynolds, D. L., Meyers, R. M., Guo, M. G., George, B. M., Mollbrink, A., Bergenstråhle, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.039 · Cited by 1,117 · see citing works
“FERMT1 (also known as kindlin-1) directly binds the cytoplasmic tail of b1 integrin to enable signaling and mediate cell spreading and controls murine cutaneous stem cell homeostasis (Kloeker et al., 2004; Larjava et al., 2008; Rognoni et al., 2014).”
BackgroundPhysical influences of the extracellular environment on cell migration
Charras, G., & Sahai, E. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3897 · Cited by 678 · see citing works
Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
Svensson, L. M., Howarth, K. M., McDowall, A., Patzak, I. M., Evans, R., Ussar, S., Moser, M., Metìn, A., Fried, M., Tomlinson, I. P. M., et al. (2009) · Nature Medicine · doi:10.1038/nm.1931 · Cited by 418 · see citing works
The insider's guide to leukocyte integrin signalling and function
Hogg, N., Patzak, I. M., & Willenbrock, F. W. (2011) · Nature reviews. Immunology · doi:10.1038/nri2986 · Cited by 402 · see citing works
McEver, R. P., & Zhu, C. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113238 · Cited by 380 · see citing works
A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans
Malinin, N. L., Zhang, L., Choi, J., Ciocea, A., Razorenova, O. V., Ma, Y.-Q., Podrez, E. A., Tosi, M. F., Lennon, D. P., Caplan, A. I., et al. (2009) · Nature Medicine · doi:10.1038/nm.1917 · Cited by 339 · see citing works
Self-citationHarburger, D. S., Bouaouina, M., & Calderwood, D. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809233200 · Cited by 304 · see citing works
Integrins and Integrin-Associated Proteins in the Cardiac Myocyte
Israeli‐Rosenberg, S., Manso, A. M., Okada, H., & Ross, R. S. (2014) · Circulation Research · doi:10.1161/circresaha.114.301275 · Cited by 239 · see citing works
Koivisto, L., Heino, J., Häkkinen, L., & Larjava, H. (2013) · Advances in Wound Care · doi:10.1089/wound.2013.0436 · Cited by 234 · see citing works
Self-citationProtons make tumor cells move like clockwork
Stock, C. M., & Schwab, A. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0677-8 · Cited by 228 · see citing works
Integrins in platelet activation
Nieswandt, B., Varga-Szabó, D., & Elvers, M. (2009) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2009.03370.x · Cited by 215 · see citing works
SHARPIN is an endogenous inhibitor of β1-integrin activation
Rantala, J. K., Pouwels, J., Pellinen, T., Veltel, S., Laasola, P., Mattila, E., Potter, C. S., Duffy, T., Sundberg, J. P., Kallioniemi, O., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2340 · Cited by 201 · see citing works
Coordinated integrin activation by actin-dependent force during T-cell migration
Nordenfelt, P., Elliott, H. L., & Springer, T. A. (2016) · Nature Communications · doi:10.1038/ncomms13119 · Cited by 172 · see citing works
Schmidt, 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 165 · see citing works
Integrins and integrin-related proteins in cardiac fibrosis
Chen, C., Li, R., Ross, R. S., & Manso, A. M. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.11.010 · Cited by 162 · see citing works
Integrin αvβ6: Structure, function and role in health and disease
Koivisto, L., Bi, J., Häkkinen, L., & Larjava, H. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.04.013 · Cited by 159 · see citing works
Self-citationUnique and redundant functions of integrins in the epidermis
Margadant, C., Charafeddine, R. A., & Sonnenberg, A. (2010) · The FASEB Journal · doi:10.1096/fj.09-151449 · Cited by 157 · see citing works
Structure of a double ubiquitin‐like domain in the talin head: a role in integrin activation
Goult, B. T., Bouaouina, M., Elliott, P. R., Bate, N., PATEL, B., Gingras, A. R., Grossmann, J. G., Roberts, G. C. K., Calderwood, D., Critchley, D. R., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.4 · Cited by 151 · see citing works
Integrin Cytoplasmic Tail Interactions
Morse, E. M., Brahme, N. N., & Calderwood, D. (2014) · Biochemistry · doi:10.1021/bi401596q · Cited by 150 · see citing works
Cell–matrix adhesion of podocytes in physiology and disease
Sachs, N., & Sonnenberg, A. (2013) · Nature Reviews Nephrology · doi:10.1038/nrneph.2012.291 · Cited by 148 · see citing works
The Importance of Podocyte Adhesion for a Healthy Glomerulus
Lennon, R., Randles, M. J., & Humphries, M. J. (2014) · Frontiers in Endocrinology · doi:10.3389/fendo.2014.00160 · Cited by 146 · see citing works
Kindler syndrome: Extension of FERMT1 mutational spectrum and natural history
Has, C., Castiglia, D., Río, M. D., Diez, M. G., Piccinni, E., Kiritsi, D., Kohlhase, J., Itin, P. H., Martin, L., Fischer, J., et al. (2011) · Human Mutation · doi:10.1002/humu.21576 · Cited by 134 · see citing works
Extracellular Matrix Stiffness: New Areas Affecting Cell Metabolism
Ge, H., Tian, M., Pei, Q., Tan, F., & Pei, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.631991 · Cited by 134 · see citing works
Integrin bi‐directional signaling across the plasma membrane
Hu, P., & Luo, B. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24154 · Cited by 132 · see citing works
Kindlin-2 links mechano-environment to proline synthesis and tumor growth
Guo, L., Cui, C., Zhang, K., Wang, J., Wang, Y., Lu, Y., Chen, K., Yuan, J., Xiao, G., Tang, B. H., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-08772-3 · Cited by 132 · see citing works
Self-citationThe Janus-like role of proline metabolism in cancer
Burke, L. E. C.-A., Guterman, I., Palacios-Gallego, R., Britton, R. G., Burschowsky, D., Tufarelli, C., & Rufini, A. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00341-8 · Cited by 128 · see citing works
Dense fibrillar collagen is a potent inducer of invadopodia via a specific signaling network
Artym, V. V., Swatkoski, S., Matsumoto, K., Campbell, C. B., Petrie, R. J., Dimitriadis, E. K., Li, X., Mueller, S. C., Bugge, T. H., Guček, M., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201405099 · Cited by 126 · see citing works
Epithelial Integrins with Special Reference to Oral Epithelia
Larjava, H., Koivisto, L., Häkkinen, L., & Heino, J. (2011) · Journal of Dental Research · doi:10.1177/0022034511402207 · Cited by 124 · see citing works
Self-citationMechanism of integrin activation by talin and its cooperation with kindlin
Lü, F., Zhu, L., Bromberger, T., Yang, J., Yang, Q., Liu, J., Plow, E. F., Moser, M., & Qin, J. (2022) · Nature Communications · doi:10.1038/s41467-022-30117-w · Cited by 119 · see citing works
Self-citationKindlin-2 controls TGF-β signalling and Sox9 expression to regulate chondrogenesis
Wu, C., Jiao, H., Lai, Y., Zheng, W., Chen, K., Qu, H., Deng, W., Song, P., Zhu, K., Cao, H., et al. (2015) · Nature Communications · doi:10.1038/ncomms8531 · Cited by 120 · see citing works
Self-citationSyndecan-1 couples the insulin-like growth factor-1 receptor to inside-out integrin activation
Beauvais, D. M., & Rapraeger, A. C. (2010) · Journal of Cell Science · doi:10.1242/jcs.067645 · Cited by 119 · see citing works
Osteoblast mineralization requires β1 integrin/ICAP-1–dependent fibronectin deposition
Brunner, M., Millon‐Frémillon, A., Chevalier, G., Nakchbandi, I. A., Mosher, D. F., Block, M. R., Albigès‐Rizo, C., & Bouvard, D. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201007108 · Cited by 118 · see citing works
Development and assessment of oligonucleotide microarrays for Atlantic salmon (Salmo salar L.)
Krasnov, A., Timmerhaus, G., Afanasyev, S., & Jørgensen, S. M. (2010) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2010.04.006 · Cited by 115 · see citing works
Liu, C.-C., Cai, D.-L., Sun, F., Wu, Z.-H., Yue, B., Zhao, S.-L., Wu, X.-S., Zhang, M., Zhu, X.-W., Peng, Z.-H., et al. (2016) · Oncogene · doi:10.1038/onc.2016.339 · Cited by 112 · see citing works
Rap1, a mercenary among the Ras-like GTPases
Frische, E. W., & Zwartkruis, F. J. T. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2009.12.043 · Cited by 113 · see citing works
A Rising Star in Pancreatic Diseases: Pancreatic Stellate Cells
Xue, R., Jia, K., Wang, J., Yang, L., Wang, Y., Gao, L., & Hao, J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00754 · Cited by 112 · see citing works
Kindlin-2 directly binds actin and regulates integrin outside-in signaling
Bledzka, K., Bialkowska, K., Sossey-Alaoui, K., Vaynberg, J., Pluskota, E., Qin, J., & Plow, E. F. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201501006 · Cited by 107 · see citing works
Self-citationQu, H., Tu, Y., Shi, X., Larjava, H., Saleem, M. A., Shattil, S. J., Fukuda, K., Qin, J., Kretzler, M., & Wu, C. (2011) · Journal of Cell Science · doi:10.1242/jcs.076976 · Cited by 107 · see citing works
Self-citationMeissner, B., Warner, A., Wong, K., Dube, N., Lorch, A. H., McKay, S., Khattra, J. S., Rogalski, T. M., Somasiri, A. M., Chaudhry, I., et al. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000537 · Cited by 103 · see citing works
Białkowska, K., Ma, Y., Bledzka, K. M., Sossey‐Alaoui, K., Izem, L., Zhang, X., Malinin, N. L., Qin, J., Byzova, T. V., & Plow, E. F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.085746 · Cited by 107 · see citing works
Self-citationOsteoblast mineralization requires β1 integrin/ICAP-1–dependent fibronectin deposition
Brunner, M., Millon‐Frémillon, A., Chevalier, G., Nakchbandi, I. A., Mosher, D. F., Block, M. R., Albigès‐Rizo, C., & Bouvard, D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.20100710804302013c · Cited by 100 · see citing works
Alon, R., & Shulman, Z. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.12.007 · Cited by 97 · see citing works
Kindlin-2 Mediates Activation of TGF-β/Smad Signaling and Renal Fibrosis
Wei, X., Xia, Y., Li, F., Tang, Y., Nie, J., Liu, Y., Zhou, Z., Zhang, H., & Hou, F. F. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012101041 · Cited by 96 · see citing works
The Structure of the N-Terminus of Kindlin-1: A Domain Important for αIIbβ3 Integrin Activation
Goult, B. T., Bouaouina, M., Harburger, D. S., Bate, N., PATEL, B., Anthis, N. J., Campbell, I. D., Calderwood, D., Barsukov, I., Roberts, G. C. K., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.061 · Cited by 95 · see citing works
Kindling the flame of integrin activation and function with kindlins
Plow, E. F., Qin, J., & Byzova, T. V. (2009) · Current Opinion in Hematology · doi:10.1097/moh.0b013e32832ea389 · Cited by 95 · see citing works
Self-citationDefects in the Leukocyte Adhesion Cascade
Etzioni, A. (2009) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-009-8132-3 · Cited by 95 · see citing works
The role of kindlins in cell biology and relevance to human disease
Lai-Cheong, J. E., Parsons, M., & McGrath, J. A. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.10.015 · Cited by 92 · see citing works
Role of the Focal Adhesion Protein Kindlin-1 in Breast Cancer Growth and Lung Metastasis
Sin, S., Bonin, F., Petit, V., Meseure, D., Lallemand, F., Bièche, I., Bellahcène, A., Castronovo, V., Wever, O. D., Gespach, C. P., et al. (2011) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djr290 · Cited by 91 · see citing works
Genetic etiologies of leukocyte adhesion defects
Etzioni, A. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.07.005 · Cited by 90 · see citing works
Significance of Talin in Cancer Progression and Metastasis
Desiniotis, A., & Kyprianou, N. (2011) · International review of cytology · doi:10.1016/b978-0-12-386039-2.00004-3 · Cited by 87 · see citing works
FERM proteins in animal morphogenesis
Tepaß, U. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.05.006 · Cited by 88 · see citing works
Kindlin-2 regulates mesenchymal stem cell differentiation through control of YAP1/TAZ
Guo, L., Cai, T., Chen, K., Wang, R., Wang, J., Cui, C., Yuan, J., Zhang, K., Liu, Z., Deng, Y., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201612177 · Cited by 87 · see citing works
Self-citationKindlin-1 Is Required for RhoGTPase-Mediated Lamellipodia Formation in Keratinocytes
Has, C., Herz, C., Павловна, З. Е., Qu, H.-Y., He, Y., Zhang, Z., Wen, T.-T., Gache, Y., Aumailley, M., & Bruckner‐Tuderman, L. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090203 · Cited by 84 · see citing works
McDowall, A., Svensson, L. M., Stanley, P., Patzak, I. M., Chakravarty, P., Howarth, K. M., Sabnis, H. S., Briones, M. A., & Hogg, N. (2010) · Blood · doi:10.1182/blood-2009-08-238709 · Cited by 81 · see citing works
Integrin Structure and Function
Srichai, M. B., & Zent, R. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0814-8_2 · Cited by 78 · see citing works
Selig, M., Lauer, J. C., Hart, M. L., & Rolauffs, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155399 · Cited by 78 · see citing works
Sossey‐Alaoui, K., Pluskota, E., Davuluri, G., Białkowska, K., Das, M., Szpak, D., Lindner, D. J., Downs-Kelly, E. P., Thompson, C. L., & Plow, E. F. (2014) · The FASEB Journal · doi:10.1096/fj.13-244004 · Cited by 77 · see citing works
Self-citationFocal Contact and Hemidesmosomal Proteins in Keratinocyte Migration and Wound Repair
Hopkinson, S. B., Hamill, K. J., Wu, Y., Eisenberg, J. L., Hiroyasu, S., & Jones, J. (2013) · Advances in Wound Care · doi:10.1089/wound.2013.0489 · Cited by 77 · see citing works
Critical Role of Filamin-binding LIM Protein 1 (FBLP-1)/Migfilin in Regulation of Bone Remodeling
Xiao, G., Cheng, H., Cao, H., Chen, K., Tu, Y., Yu, S., Jiao, H., Yang, S., Im, H., Chen, D., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.331249 · Cited by 71 · see citing works
Self-citationKindlin supports platelet integrin αIIbβ3 activation by interacting with paxillin
Gao, J., Huang, M., Lai, J., Mao, K., Sun, P., Cao, Z., Hu, Y., Zhang, Y., Schulte, M. L., Jin, C., et al. (2017) · Journal of Cell Science · doi:10.1242/jcs.205641 · Cited by 66 · see citing works
Structural and biophysical properties of the integrin-associated cytoskeletal protein talin
Roberts, G. C. K., & Critchley, D. R. (2009) · Biophysical Reviews · doi:10.1007/s12551-009-0009-4 · Cited by 65 · see citing works
Fukuda, K., Bledzka, K. M., Yang, J., Perera, H., Plow, E. F., & Qin, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.596692 · Cited by 65 · see citing works
Self-citationMechanisms of Platelet Activation and Integrin αIIβ3
Joo, S. (2012) · Korean Circulation Journal · doi:10.4070/kcj.2012.42.5.295 · Cited by 64 · see citing works
Shen, Z., Ye, Y., Dong, L.-Y., Vainionpää, S., Mustonen, H. K., Puolakkainen, P. A., & Wang, S. (2011) · The American Journal of Surgery · doi:10.1016/j.amjsurg.2011.06.050 · Cited by 64 · see citing works
Kindlin-2 haploinsufficiency protects against fatty liver by targeting Foxo1 in mice
Gao, H., Zhou, L. F., Zhong, Y., Ding, Z., Lin, S., Hou, X., Zhou, X., Shao, J., Yang, F., Zou, X., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28692-z · Cited by 63 · see citing works
Huet-Calderwood, C., Brahme, N. N., Kumar, N., Stiegler, A. L., Raghavan, S., Boggon, T. J., & Calderwood, D. (2014) · Journal of Cell Science · doi:10.1242/jcs.155879 · Cited by 63 · see citing works
Li, R., & Frangogiannis, N. G. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.07.006 · Cited by 62 · see citing works
miR-138–Mediated Regulation of KINDLIN-2 Expression Modulates Sensitivity to Chemotherapeutics
Sossey‐Alaoui, K., & Plow, E. F. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0299 · Cited by 58 · see citing works
Self-citationGrainyhead-like 2 downstream targets act to suppress EMT during neural tube closure
Ray, H. J., & Niswander, L. A. (2016) · Development · doi:10.1242/dev.129825 · Cited by 57 · see citing works
Smurf1 inhibits integrin activation by controlling Kindlin-2 ubiquitination and degradation
Wei, X., Wang, X., Zhan, J., Chen, Y., Fang, W., Zhang, L., & Zhang, H. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201609073 · Cited by 57 · see citing works
Kindlin-2 in pancreatic stellate cells promotes the progression of pancreatic cancer
Yoshida, N., Masamune, A., Hamada, S., Kikuta, K., Takikawa, T., Motoi, F., Unno, M., & Shimosegawa, T. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.008 · Cited by 56 · see citing works
Feigelson, S. W., Grabovsky, V., Manevich, E., Pasvolsky, R., Shulman, Z., Shinder, V., Klein, E., Etzioni, A., Aker, M., & Alon, R. (2011) · Blood · doi:10.1182/blood-2010-12-322859 · Cited by 53 · see citing works
Role of integrins in the periodontal ligament: organizers and facilitators
Barczyk, M. M., Bolstad, A. I., & Gullberg, D. (2013) · Periodontology 2000 · doi:10.1111/prd.12027 · Cited by 56 · see citing works
Uncovering functional differences between kindlin-1 and kindlin-2 in keratinocytes
Bandyopadhyay, A., Rothschild, G., Kim, S., Calderwood, D., & Raghavan, S. (2012) · Journal of Cell Science · doi:10.1242/jcs.096214 · Cited by 52 · see citing works
Blumbach, K., Zweers, M. C., Brunner, G., Peters, A. S., Schmitz, M., Schulz, J.-N., Schild, A., Denton, C. P., Sakai, T., Fässler, R., et al. (2010) · Journal of Cell Science · doi:10.1242/jcs.063024 · Cited by 52 · see citing works
The NPIY motif in the integrin β1 tail dictates the requirement for talin-1 in outside-in signaling
Nieves, B., Jones, C. W., Ward, R., Ohta, Y., Reverte, C. G., & LaFlamme, S. E. (2010) · Journal of Cell Science · doi:10.1242/jcs.056549 · Cited by 52 · see citing works
Opposite Role of Kindlin-1 and Kindlin-2 in Lung Cancers
Zhan, J., Zhu, X., Guo, Y., Wang, Y., Wang, Y., Qiang, G., Niu, M., Hu, J., Du, J., Li, Z., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050313 · Cited by 50 · see citing works
Zhang, X., WU, J. M., Luo, S., Lechler, T., & Zhang, J. Y. (2016) · Oncotarget · doi:10.18632/oncotarget.9110 · Cited by 50 · see citing works
Sossey‐Alaoui, K., Pluskota, E., Szpak, D., Schiemann, W. P., & Plow, E. F. (2018) · Scientific Reports · doi:10.1038/s41598-018-25373-0 · Cited by 50 · see citing works
Self-citationThe Serine/Threonine Kinase Ndr2 Controls Integrin Trafficking and Integrin-Dependent Neurite Growth
Rehberg, K., Kliche, S., Madencioglu, D. A., Thiere, M., Müller, B., Meineke, B. M., Freund, C., Budinger, E., & Stork, O. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.2728-13.2014 · Cited by 49 · see citing works
Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion
Zhu, L., Liu, H., Lü, F., Yang, J., Byzova, T. V., & Qin, J. (2019) · Structure · doi:10.1016/j.str.2019.09.006 · Cited by 49 · see citing works
Pluskota, E., Ma, Y., Bledzka, K. M., Białkowska, K., Soloviev, D. A., Szpak, D., Podrez, E. A., Fox, P. L., Hazen, S. L., Dowling, J. J., et al. (2013) · Blood · doi:10.1182/blood-2013-04-497669 · Cited by 48 · see citing works
Self-citationXu, Z., Chen, X., Zhi, H., Gao, J., Białkowska, K., Byzova, T. V., Pluskota, E., White, G., Liu, J., Plow, E. F., et al. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.303851 · Cited by 48 · see citing works
Self-citationStromal regulation of embryonic and postnatal mammary epithelial development and differentiation
Howard, B. A., & Lu, P. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2014.01.004 · Cited by 49 · see citing works
Role of Kindlin-2 in Fibroblast Functions: Implications for Wound Healing
He, Y., Esser, P. R., Schacht, V., Bruckner‐Tuderman, L., & Has, C. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.273 · Cited by 47 · see citing works
Lai‐Cheong, J. E., Parsons, M., Tanaka, A., Ussar, S., South, A. P., Sethuraman, G., Mee, J. B., Barbaroux, J.-B., Techanukul, T., Almaani, N., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.081154 · Cited by 46 · see citing works
Kindlin-2 modulates MafA and β-catenin expression to regulate β-cell function and mass in mice
Zhu, K., Lai, Y., Cao, H., Bai, X., Liu, C.-J., Yan, Q., Ma, L., Chen, D., Kanaporis, G., Wang, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14186-y · Cited by 46 · see citing works
Self-citationKindlin-1 and -2 Have Overlapping Functions in Epithelial Cells
He, Y., Esser, P. R., Heinemann, A., Bruckner‐Tuderman, L., & Has, C. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.053 · Cited by 46 · see citing works
Sun, Y., Guo, C., Ma, P., Lai, Y., Yang, F., Cai, J., Cheng, Z., Zhang, K., Liu, Z., Tian, Y., et al. (2017) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016091021 · Cited by 44 · see citing works
Self-citationIntegrin Activation: Implications for Axon Regeneration
Cheah, M., & Andrews, M. R. (2018) · Cells · doi:10.3390/cells7030020 · Cited by 45 · see citing works
Integrins and extracellular matrix in mechanotransduction
Ramage, L. (2011) · Cell Health and Cytoskeleton · doi:10.2147/chc.s21829 · Cited by 44 · see citing works
Overview of Integrin Signaling in the Immune System
Kinashi, T. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-166-6_17 · Cited by 45 · see citing works
Integrins in periodontal disease
Larjava, H., Koivisto, L., Heino, J., & Häkkinen, L. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.03.010 · Cited by 43 · see citing works
Self-citationQu, H., Tu, Y., Guan, J.-L., Xiao, G., & Wu, C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.580811 · Cited by 43 · see citing works
Self-citationKindlin-1 contributes to EGF-induced re-epithelialization in skin wound healing
Shen, C., Sun, L., Zhu, N., & Qi, F. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.2911 · Cited by 43 · see citing works
Talin and signaling through integrins
Bouaouina, M., Harburger, D. S., & Calderwood, D. A. (2011) · Methods in Molecular Biology · doi:10.1007/978-1-61779-166-6_20 · Cited by 42 · see citing works
Fröbel, J., Cadeddu, R., Hartwig, S., Bruns, I., Wilk, C. M., Kündgen, A., Fischer, J., Schroeder, T. A., Steidl, U. G., Germing, U., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.023168 · Cited by 42 · see citing works
Hart, R., Stanley, P., Chakravarty, P., & Hogg, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.434621 · Cited by 42 · see citing works
Kerr, B. A., & Byzova, T. V. (2010) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a001211.01 · Cited by 42 · see citing works
- Authors
- Larjava, H., Plow, E. F., & Wu, C.
- Affiliations
- University of British Columbia (CA)
- Cleveland Clinic (US)
- University of Pittsburgh (US)
- Venue
- The EMBO Reports
- Published
- 2008-11-07
- Volume
- 9
- Issue
- 12
- Pages
- 1203-1208
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC2603460
- OpenAlex
- W2159437476
- Cited by
- 268
- References
- 49
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 7 · 2023: 7 · 2022: 14 · 2021: 16 · 2020: 12 · 2019: 13 · 2018: 11 · 2017: 15 · 2016: 10 · 2015: 12 · 2014: 21 · 2013: 21 · 2012: 16
- FWCI
- 2.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (P01HL073311)
- National Institute of General Medical Sciences (GM 65188, R01GM065188)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK54639, R01DK054639)
- National Institute of Dental and Craniofacial Research (R01DE016099, DE016099)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Keywords
- kindlin, integrin signaling, cell-matrix adhesion, talin, integrin activation, integrin-linked kinase, cytoskeletal organization, Kindler syndrome, kindlin-1, Kindlin-2, kindlin-3, embryonic lethality
- MeSH terms
- Animals, Carrier Proteins, Cell Adhesion, Disease, Humans, Signal Transduction, Integrins, Cell-Matrix Junctions
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
