Kindlins: essential regulators of integrin signalling and cell-matrix adhesion

Untitled work

Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606

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

Inside Out

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

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

The Talin Head Domain Binds to Integrin β Subunit Cytoplasmic Tails and Regulates Integrin Activation

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

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

SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function

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

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

Structure of the ERM Protein Moesin Reveals the FERM Domain Fold Masked by an Extended Actin Binding Tail Domain

Pearson, M. A., Reczek, D., Bretscher, A. P., & Karplus, P. A. (2000) · Cell · doi:10.1016/s0092-8674(00)80836-3 · Cited by 614

Breaking the Integrin Hinge

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

Matrikines and the lungs

Burgess, J. K., & Weckmann, M. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.02.002 · Cited by 43

Of Kindlins and Cancer

Plow, E. F., Das, M., Białkowska, K., & Sossey‐Alaoui, K. (2016) · Discoveries · doi:10.15190/d.2016.6 · Cited by 40

Kindlin-2 mediates mechanotransduction in bone by regulating expression of Sclerostin in osteocytes

Qin, L., Fu, X., Ma, J., Lin, M., Zhang, P., Wang, Y., Yan, Q., Tao, C., Liu, W., Tang, B. H., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-01950-4 · Cited by 41

Drosophila integrin adhesion complexes are essential for hemocyte migration in vivo

Moreira, C. G. A., Jacinto, A., & Prag, S. (2013) · Biology Open · doi:10.1242/bio.20134564 · Cited by 40

Phosphatidylinositol 3-Kinase/Akt Mediates Integrin Signaling To Control RNA Polymerase I Transcriptional Activity

Wu, C., You, J., Fu, J., Wang, X., & Zhang, Y. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00004-16 · Cited by 38

Kindler Syndrome Pathogenesis and Fermitin Family Homologue 1 (Kindlin-1) Function

D'Souza, M., Kimble, R. M., & McMillan, J. R. (2009) · Dermatologic Clinics · doi:10.1016/j.det.2009.10.012 · Cited by 38

Kindlin-2 controls sensitivity of prostate cancer cells to cisplatin-induced cell death

Gong, X., An, Z., Wang, Y., Guan, L., Fang, W., Strömblad, S., Jiang, Y., & Zhang, H. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.08.003 · Cited by 39

Migfilin Interacts with Src and Contributes to Cell-Matrix Adhesion-mediated Survival Signaling

Zhao, J., Zhang, Y., Ithychanda, S. S., Tu, Y., Chen, K., Qin, J., & Wu, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.045021 · Cited by 37

Kindlin-2 promotes genome instability in breast cancer cells

Zhao, T., Guan, L., Yu, Y., Pei, X., Zhan, J., Han, L., Tang, Y., Li, F., Fang, W., & Zhang, H. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.11.043 · Cited by 38

The Kindlin2-p53-SerpinB2 signaling axis is required for cellular senescence in breast cancer

Sossey‐Alaoui, K., Pluskota, E., Szpak, D., & Plow, E. F. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1774-z · Cited by 38

Talin1 Regulates Integrin Turnover To Promote Embryonic Epithelial Morphogenesis

Liu, J., He, X., Qi, Y., Tian, X., Monkley, S. J., Critchley, D. R., Corbett, S., Lowry, S. F., Graham, A. M., & Li, S. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01403-10 · Cited by 36

The β3 integrin cytoplasmic tail: protein scaffold and control freak

Shattil, S. J. (2009) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2009.03397.x · Cited by 35

Kindlin-1 Regulates Integrin Dynamics and Adhesion Turnover

Margadant, C., Kreft, M., Zambruno, G., & Sonnenberg, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065341 · Cited by 35

Partial Loss of Epithelial Phenotype in Kindlin-1–Deficient Keratinocytes

Qu, H., Wen, T.-T., Pesch, M., & Aumailley, M. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.01.005 · Cited by 36

Phosphatidylcholine passes through lateral tight junctions for paracellular transport to the apical side of the polarized intestinal tumor cell-line CaCo2

Stremmel, W., Staffer, S., Gan‐Schreier, H., Wannhoff, A., Bach, M., & Gauss, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.06.019 · Cited by 35

Kindlin‐2 interacts with endothelial adherens junctions to support vascular barrier integrity

Pluskota, E., Bledzka, K. M., Białkowska, K., Szpak, D., Soloviev, D. A., Jones, S. V., Verbovetskiy, D., & Plow, E. F. (2017) · The Journal of Physiology · doi:10.1113/jp274380 · Cited by 35

Kindlin-2 regulates hepatic stellate cells activation and liver fibrogenesis

Yu, J., Hu, Y., Gao, Y., Li, Q., Zeng, Z., Li, Y., & Chen, H. (2018) · Cell Death Discovery · doi:10.1038/s41420-018-0095-9 · Cited by 35

Hemidesmosomes and Focal Adhesions Treadmill as Separate but Linked Entities during Keratinocyte Migration

Pora, A., Yoon, S., Windoffer, R., & Leube, R. E. (2019) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2019.03.1139 · Cited by 35

Mitochondrial metabolism and cancer metastasis

Yu, D., Liu, C., & Guo, L. (2020) · Annals of Translational Medicine · doi:10.21037/atm.2020.03.42 · Cited by 34

Dynamic interactions between cells and their extracellular matrix mediate embryonic development

Goody, M. F., & Henry, C. A. (2010) · Molecular Reproduction and Development · doi:10.1002/mrd.21157 · Cited by 34

Src-mediated phosphorylation converts FHL1 from tumor suppressor to tumor promoter

Wang, X., Wei, X.-F., Yuan, Y., Sun, Q., Zhan, J., Zhang, J., Tang, Y., Li, F., Ding, L., Ye, Q., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201708064 · Cited by 31

Talin and kindlin cooperate to control the density of integrin clusters

Pernier, J., Santos, M. C. D., Souissi, M., Joly, A., Narassimprakash, H., Rossier, O., Giannone, G., Helfer, E., Sengupta, K., & Clainche, C. L. (2023) · Journal of Cell Science · doi:10.1242/jcs.260746 · Cited by 32

Role of Kindlin-2 in cancer progression and metastasis

Wang, W., Kansakar, U., Marković, V. G., & Sossey‐Alaoui, K. (2020) · Annals of Translational Medicine · doi:10.21037/atm.2020.03.64 · Cited by 31

A feedback regulation between Kindlin‐2 and GLI1 in prostate cancer cells

Gao, J., Khan, A. A., Shimokawa, T., Zhan, J., Strömblad, S., Fang, W., & Zhang, H. (2013) · FEBS Letters · doi:10.1016/j.febslet.2012.12.028 · Cited by 32

Talin and Kindlin as Integrin-Activating Proteins: Focus on the Heart

Chen, C., Manso, A. M., & Ross, R. S. (2019) · Pediatric Cardiology · doi:10.1007/s00246-019-02167-3 · Cited by 32

Emerging evidence for kindlin oligomerization and its role in regulating kindlin function

Bu, W., Levitskaya, Z., Tan, S., & Gao, Y. (2021) · Journal of Cell Science · doi:10.1242/jcs.256115 · Cited by 30

Kindlin-2 inhibits serous epithelial ovarian cancer peritoneal dissemination and predicts patient outcomes

Ren, C., Du, J., Xi, C., Yu, Y., Hu, A., Zhan, J., Guo, H., Fang, W., Liu, C., & Zhang, H. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.02.087 · Cited by 28

Kindlin-2 Acts as a Key Mediator of Lung Fibroblast Activation and Pulmonary Fibrosis Progression

Zhang, P., Wang, J., Luo, W., Yuan, J., Cui, C., Guo, L., & Wu, C. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2020-0320oc · Cited by 28

Function of liprins in cell motility

de Curtis, I. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.09.014 · Cited by 29

Kindlin‐2 phosphorylation by Src at Y193 enhances Src activity and is involved in Migfilin recruitment to the focal adhesions

Liu, Z., Lu, D., Wang, X., Wan, J., Liu, C., & Zhang, H. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.05.038 · Cited by 29

Copy Number Variants in miR-138 as a Potential Risk Factor for Early-Onset Alzheimer’s Disease

Boscher, E., Husson, T., Quenez, O., Laquerrière, A., Marguet, F., Cassinari, K., Wallon, D., Martinaud, O., Charbonnier, C., Nicolas, G., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180940 · Cited by 27

YBX1 knockdown induces renal cell carcinoma cell apoptosis via Kindlin-2

Cui, Q., Wang, C., Liu, S., Du, R., Tian, S., Chen, R., Geng, H., Subramanian, S., Niu, Y., Wang, Y., et al. (2021) · Cell Cycle · doi:10.1080/15384101.2021.1985771 · Cited by 27

Leukocyte adhesion deficiency syndrome: a controversy solved

Abram, C. L., & Lowell, C. A. (2009) · Immunology and Cell Biology · doi:10.1038/icb.2009.32 · Cited by 27

Optogenetic interrogation of integrin αVβ3 function in endothelial cells

Liao, Z., Kasirer‐Friede, A., & Shattil, S. J. (2017) · Journal of Cell Science · doi:10.1242/jcs.205203 · Cited by 27

Kindlin-2: A novel prognostic biomarker for patients with hepatocellular carcinoma

Ge, Y., Liu, D., Jia, W., Li, J., Ma, J., Yu, J.-H., & Xu, G. (2014) · Pathology - Research and Practice · doi:10.1016/j.prp.2014.09.011 · Cited by 26

Structure basis of the FERM domain of kindlin-3 in supporting integrin αIIbβ3 activation in platelets

Sun, J., Xiao, D., Ni, Y., Zhang, T., Cao, Z., Zhou, X., Nguyen, H., Zhang, J., White, G., Ding, J., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020001575 · Cited by 26

Focal adhesion molecule Kindlin-1 mediates activation of TGF-β signaling by interacting with TGF-βRI, SARA and Smad3 in colorectal cancer cells

Kong, J., Du, J., Wang, Y., Yang, M., Gao, J., Wei, X., Fang, W., Zhan, J., & Zhang, H. (2016) · Oncotarget · doi:10.18632/oncotarget.12779 · Cited by 27

Epidermolysis Bullosa—A Different Genetic Approach in Correlation with Genetic Heterogeneity

Pânzaru, M.-C., Caba, L., Florea, L., Braha, E. E., & Gorduza, E. V. (2022) · Diagnostics · doi:10.3390/diagnostics12061325 · Cited by 25

Molecular mechanisms of heart failure: insights from Drosophila

Zhu, S., Han, Z., Luo, Y. H., Chen, Y., Zeng, Q., Wu, X., & Yuan, W. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9590-3 · Cited by 26

The extreme C-terminal region of kindlin-2 is critical to its regulation of integrin activation

Hirbawi, J., Białkowska, K., Bledzka, K. M., Liu, J., Fukuda, K., Qin, J., & Plow, E. F. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.776195 · Cited by 25

Kindlin-2 Mediates Mechanical Activation of Cardiac Myofibroblasts

Godbout, E., Son, D. O., Hume, S., Boo, S., Sarrazy, V., Clément, S., Kapùs, A., Wehrle‐Haller, B., Bruckner‐Tuderman, L., Has, C., et al. (2020) · Cells · doi:10.3390/cells9122702 · Cited by 23

Induction of senescence pathways in Kindler syndrome primary keratinocytes

Piccinni, E., Zenzo, G. D., Maurelli, R., Dellambra, E., Teson, M., Has, C., Zambruno, G., & Castiglia, D. (2012) · British Journal of Dermatology · doi:10.1111/bjd.12184 · Cited by 24

Localization and potential function of kindlin‐1 in periodontal tissues

Petricca, G., Leppilampi, M., Jiang, G., Owen, G., Wiebe, C., Tu, Y., Koivisto, L., Häkkinen, L., Wu, C., & Larjava, H. (2009) · European Journal Of Oral Sciences · doi:10.1111/j.1600-0722.2009.00651.x · Cited by 24

Kindlin-3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells

Qu, J., Ero, R., Chen, F., Ong, L.-T., Tan, H., Lee, H.-S., Ismail, M. H., Bu, W., Nama, S., Sampath, P., et al. (2015) · Scientific Reports · doi:10.1038/srep18491 · Cited by 24

Kindlin-1 Regulates Epidermal Growth Factor Receptor Signaling

Michael, M., Begum, R., Chan, G. K., Whitewood, A. J., Matthews, D. R., Goult, B. T., McGrath, J. A., & Parsons, M. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.08.020 · Cited by 23

Intercellular adhesion molecule 1: Recent findings and new concepts involved in mammalian spermatogenesis

Mruk, D. D., Xiao, X., Łydka, M., Li, M., Bilińska, B., & Cheng, C. Y. (2013) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.07.003 · Cited by 23

Expression of Kindlin-1 in human hepatocellular carcinoma and its prognostic significance

Ma, H., Shu, Q.-H., Pan, J., Liu, D., Xu, G., Li, J., Ma, J.-L., Jia, W., Yv, J.-H., & Ge, Y. (2015) · Tumor Biology · doi:10.1007/s13277-015-3060-8 · Cited by 22

Kindlin-2 Expression in Peritumoral Stroma Is Associated With Poor Prognosis in Pancreatic Ductal Adenocarcinoma

Mahawithitwong, P., Ohuchida, K., Ikenaga, N., Fujita, H., Zhao, M., Kozono, S., Shindo, K., Ohtsuka, T., Mizumoto, K., & Tanaka, M. (2013) · Pancreas · doi:10.1097/mpa.0b013e318279bd66 · Cited by 22

Mild Clinical Phenotype of Kindler Syndrome Associated with Late Diagnosis and Skin Cancer

Has, C., Burger, B., Volz, A., Kohlhase, J., Bruckner‐Tuderman, L., & Itin, P. H. (2010) · Dermatology · doi:10.1159/000320235 · Cited by 22

Distinct expression profiles and functions of Kindlins in breast cancer

Azorin, P., Bonin, F., Moukachar, A., Ponceau, A., Vacher, S., Bièche, I., Marangoni, E., Fuhrmann, L., Vincent‐Salomon, A., Lidereau, R., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0955-4 · Cited by 22

Optimal T Cell Activation and B Cell Antibody Responses In Vivo Require the Interaction between Leukocyte Function–Associated Antigen-1 and Kindlin-3

Morrison, V. L., Uotila, L. M., Asens, M. L., Savinko, T., & Fagerholm, S. C. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402741 · Cited by 21

IL‐1β enhances cell adhesion to degraded fibronectin

Rajshankar, D., Downey, G. P., & McCulloch, C. A. (2012) · The FASEB Journal · doi:10.1096/fj.12-207381 · Cited by 21

Effects of Smad3 on the proliferation and steroidogenesis in human ovarian luteinized granulosa cells: Role of Smad3 in Human Granulosa Cells

Liu, Y., Chen, X., Xue, X., Shen, C., Shi, C., Dong, J., Zhang, H., Liang, R., Li, S., & Xu, J. (2014) · IUBMB Life · doi:10.1002/iub.1280 · Cited by 20

Sharpin suppresses β1-integrin activation by complexing with the β1 tail and kindlin-1

Gao, J., Bao, Y., Ge, S., Sun, P., Sun, J., Liu, J., Chen, F., Han, L., Cao, Z., Qin, J., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0407-6 · Cited by 20

Integrin Regulators in Neutrophils

Pulikkot, S., Hu, L., Chen, Y., Sun, H., & Fan, Z. (2022) · Cells · doi:10.3390/cells11132025 · Cited by 21

Emergence and subsequent functional specialization of kindlins during evolution of cell adhesiveness

Meller, J., Rogozin, I. B., Poliakov, E., Meller, N., Bedanov-Pack, M., Plow, E. F., Qin, J., Podrez, E. A., & Byzova, T. V. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-08-1294 · Cited by 19

Phylogenetic Analysis of Kindlins Suggests Subfunctionalization of an Ancestral Unduplicated Kindlin into Three Paralogs in Vertebrates

Khan, A. A., Janke, A., Shimokawa, T., & Zhang, H. (2011) · Evolutionary Bioinformatics · doi:10.4137/ebo.s6179 · Cited by 19

Integrity of kindlin-2 FERM subdomains is required for supporting integrin activation

Xu, Z., Gao, J., Jiang, H., & Ma, Y. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.03.086 · Cited by 19

Phosphorylation of Kindlins and the Control of Integrin Function

Białkowska, K., Qin, J., & Plow, E. F. (2021) · Cells · doi:10.3390/cells10040825 · Cited by 18

Regulation of thymocyte trafficking by Tagap, a GAP domain protein linked to human autoimmunity

Duke‐Cohan, J. S., Ishikawa, Y., Yoshizawa, A., Choi, Y. I., Lee, C., Acuto, O., Kissler, S., & Reinherz, E. L. (2018) · Science Signaling · doi:10.1126/scisignal.aan8799 · Cited by 18

Kindlin-1 Mutant Zebrafish as an In Vivo Model System to Study Adhesion Mechanisms in the Epidermis

Postel, R., Margadant, C., Fischer, B., Kreft, M., Janssen, H., Secades, P., Zambruno, G., & Sonnenberg, A. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.154 · Cited by 18

Kindlin-2 could influence breast nodule elasticity and improve lymph node metastasis in invasive breast cancer

Xue, X., Li, J., Wan, W., Shi, X., & Zheng, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-07075-1 · Cited by 18

Kindlin-2 regulates the oncogenic activities of integrins and TGF-β in triple-negative breast cancer progression and metastasis

Yousafzai, N. A., Khalki, L. E., Wang, W., Szpendyk, J., & Sossey‐Alaoui, K. (2024) · Oncogene · doi:10.1038/s41388-024-03166-2 · Cited by 16

New intragenic and promoter region deletion mutations inFERMT1underscore genetic homogeneity in Kindler syndrome

Fuchs‐Telem, D., Nousbeck, J., Singer, A., McGrath, J. A., Sarig, O., & Sprecher, E. (2014) · Clinical and Experimental Dermatology · doi:10.1111/ced.12222 · Cited by 16

Prognostic implications of Kindlin proteins in human osteosarcoma

Ning, K., Zhang, H., Wang, Z., & Li, K. (2017) · OncoTargets and Therapy · doi:10.2147/ott.s125418 · Cited by 16

Kindlin-2 promotes rear focal adhesion disassembly and directional persistence during cell migration

Liu, J., Liu, Z., Chen, K., Chen, W., Fang, X., Li, M., Zhou, X., Ding, N., Lei, H., Chen, G., et al. (2020) · Journal of Cell Science · doi:10.1242/jcs.244616 · Cited by 17

Integrin αIIbβ3

Bledzka, K. M., Qin, J., & Plow, E. F. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813456-6.00012-6 · Cited by 16

RhoA activation by CNFy restores cell–cell adhesion in kindlin‐2‐deficient keratinocytes

He, Y., Sonnenwald, T., Sprenger, A., Hansen, U. J., Dengjel, J., Bruckner‐Tuderman, L., Schmidt, G., & Has, C. (2014) · The Journal of Pathology · doi:10.1002/path.4350 · Cited by 15

Involvement of kindlin‐2 in irisin’s protection against ischaemia reperfusion‐induced liver injury in high‐fat diet‐fed mice

Jia, Z., Ren, Y., Bi, J., Wang, M., Zhang, L., Wang, T., Wei, S., Mou, X., Lv, Y., & Wu, R. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15910 · Cited by 15

Kindlin-2 promotes Src-mediated tyrosine phosphorylation of androgen receptor and contributes to breast cancer progression

Ma, L., Tian, Y.-T., Qian, T., Li, W.-J., Liu, C.-M., Chu, B.-Z., Kong, Q., Cai, R., Bai, P., Ma, L., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04945-z · Cited by 15

Kindlin2-mediated phase separation underlies integrin adhesion formationPreprint

Li, Y., Zhang, T., Li, H., Yang, H., Lin, R., Sun, K., Wang, L., Zhang, J., Wei, Z., & Yu, C. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.10.197400 · Cited by 14

Caveolin-1 Influences LFA-1 Redistribution upon TCR Stimulation in CD8 T Cells

Borger, J. G., Morrison, V. L., Filby, A. J., Garcia, C., Uotila, L. M., Simbari, F., Fagerholm, S. C., & Zamoyska, R. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700431 · Cited by 13

Mouse Hair Cycle Expression Dynamics Modeled as Coupled Mesenchymal and Epithelial Oscillators

Tasseff, R. A., Bheda-Malge, A., DiColandrea, T., Bascom, C. C., Isfort, R. J., & Gelinas, R. E. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003914 · Cited by 13

Single-cell and bulk transcriptional profiling of mouse ovaries reveals novel genes and pathways associated with DNA damage response in oocytes

Mills, M., Emori, C., Kumar, P., Boucher, Z., George, J., & Bolcun-Filas, E. (2025) · Developmental Biology · doi:10.1016/j.ydbio.2024.09.007 · Cited by 12

Recent advances in the understanding of the molecular mechanisms regulating platelet integrin αIIbβ3 activation

Tao, L., Zhang, Y., Xi, X., & Kieffer, N. (2010) · Protein & Cell · doi:10.1007/s13238-010-0089-8 · Cited by 13

Fermitins, the Orthologs of Mammalian Kindlins, Regulate the Development of a Functional Cardiac Syncytium in Drosophila melanogaster

Catterson, J. H., Heck, M. M. S., & Hartley, P. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062958 · Cited by 12

Protein kinase D isoforms are dispensable for integrin‐mediated lymphocyte adhesion and homing to lymphoid tissues

Matthews, S. A., Lek, H. S., Morrison, V. L., MacKenzie, M. G., Zarrouk, M., Cantrell, D. A., & Fagerholm, S. C. (2012) · European Journal of Immunology · doi:10.1002/eji.201142004 · Cited by 11

Paxillin binding to the PH domain of kindlin‐3 in platelets is required to support integrin αIIbβ3 outside‐in signaling

Nguyen, H. T. T., Xu, Z., Shi, X., Liu, S., Schulte, M. L., White, G., & Ma, Y. (2021) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.15505 · Cited by 11

Chemokine arrest signals to leukocyte integrins trigger bi-directional-occupancy of individual heterodimers by extracellular and cytoplasmic ligands

Alon, R. (2010) · Cell Adhesion & Migration · doi:10.4161/cam.4.2.11133 · Cited by 11

Oligodendrocyte mechanotransduction channel TMEM63A regulates myelin sheath geometry

Dereddi, R. R., Djannatian, M., Fiore, F., Kalita, D., Verkest, C., Torres, F. B., Möbius, W., Khodaie, B., Ruhwedel, T., Alhalaseh, K., et al. (2026) · Neuron · doi:10.1016/j.neuron.2025.11.009 · Cited by 13

Kindlin-2 promotes clear cell renal cell carcinoma progression through the Wnt signaling pathway

Li, M., Pei, X., Wang, G., Zhan, J., Du, J., Jiang, H., Tang, Y., Zhang, H., & He, H. (2017) · Oncology Reports · doi:10.3892/or.2017.5789 · Cited by 10

Mechano-regulation of proline metabolism and cancer progression by kindlin-2

Guo, L., & Wu, C. (2019) · Molecular & Cellular Oncology · doi:10.1080/23723556.2019.1596003 · Cited by 10

Targeted Deletion of Kindlin-2 in Mouse Mammary Glands Inhibits Tumor Growth, Invasion, and Metastasis Downstream of a TGF-β/EGF Oncogenic Signaling Pathway

Wang, W., Rana, P. S., Alkrekshi, A., Białkowska, K., Marković, V. G., Schiemann, W. P., Plow, E. F., Pluskota, E., & Sossey‐Alaoui, K. (2022) · Cancers · doi:10.3390/cancers14030639 · Cited by 10

Advances in the Structural and Physiological Functions of SHARPIN

Yu, B., Wang, F., & Wang, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.858505 · Cited by 10

Knockdown of the KINDLIN-2 Gene and Reduced Expression of Kindlin-2 Affects Vascular Permeability in Angiogenesis in a Mouse Model of Wound Healing

Ying, J., Luan, W., Lu, L., Zhang, S., & Qi, F. (2018) · Medical Science Monitor · doi:10.12659/msm.910059 · Cited by 10

Role of CK2 in the Control of Cell Plasticity in Breast Carcinoma Progression

Filhol, O., Deshière, A., & Cochet, C. (2013) · doi:10.1002/9781118482490.ch14 · Cited by 10

FERMT1 promotes epithelial-mesenchymal transition of hepatocellular carcinoma by activating EGFR/AKT/β-catenin and EGFR/ERK pathways

Guo, W., Liu, M., Luo, W., Peng, J., Liu, F., Ma, X., Wang, L., & Yang, S. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102144 · Cited by 9

Kindlin-2 enhances c-Myc translation through association with DDX3X to promote pancreatic ductal adenocarcinoma progression

Liu, C., Jiang, K., Ding, Y., Yang, A., Cai, R., Bai, P., Xiong, M., Fu, C., Quan, M., Xiong, Z., et al. (2023) · Theranostics · doi:10.7150/thno.85421 · Cited by 10

Kindlin-2 regulates the differentiation of 3T3-L1 preadipocytes: implications for wound healing

Pan, Y., Wang, Q., Luan, W., Shi, Y., Liu, J., & Qi, F. (2021) · Annals of Translational Medicine · doi:10.21037/atm-21-176 · Cited by 9

How signaling pathways link extracellular mechano‐environment to proline biosynthesis: A hypothesis

Chen, K., Guo, L., & Wu, C. (2021) · BioEssays · doi:10.1002/bies.202100116 · Cited by 9

Kindlin-2 regulates colonic cancer stem-like cells survival and self-renewal via Wnt/β-catenin mediated pathway

Yadav, R. P., & Baranwal, S. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110953 · Cited by 10

Novel Automated Tracking Analysis of Particles Subjected to Shear Flow: Kindlin-3 Role in B Cells

Willenbrock, F. W., Zicha, D., Hoppe, A., & Hogg, N. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.06.051 · Cited by 9

Kindler-Syndrom

Has, C. (2009) · Der Hautarzt · doi:10.1007/s00105-008-1676-y · Cited by 9

ITGB1/FERMT1 mechanoactivation enhances CD44 characteristic stemness in oral squamous cell carcinoma via ubiquitin-dependent CK1α degradation

Li, X., Zhao, H., Jiang, E., Liu, P., Chen, Y., Wang, Y., Li, J., Wu, Y., Liu, Z., & Shang, Z. (2025) · Oncogene · doi:10.1038/s41388-025-03317-z · Cited by 9

Kindlin for the Fire: Targeting Proline Synthesis to Extinguish Matrix Production in Pulmonary Fibrosis

Guzy, R. D., & Redente, E. F. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2021-0137ed · Cited by 8

Progresses in The Studies on Kindlin Family Members

Xiong, Y., Xiao-Wei, G. O. N. G., & Jiang, Y. (2011) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2010.00266 · Cited by 7

Increased extracellular matrix stiffness regulates myofibroblast transformation through induction of autophagy-mediated Kindlin-2 cytoplasmic translocation

Zhao, Z., Han, W., Huang, G., He, Y., Zuo, X., Ning, M., Jiang, N., & Hong, H. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.113974 · Cited by 6

FERMT2 drives anoikis resistance and peritoneal metastasis by enhancing extracellular matrix deposition in gastric cancer

He, C., Zhou, Z. Y., Yang, Y., Zhu, S., Wang, H., & Teng, L. (2025) · Gastric Cancer · doi:10.1007/s10120-025-01602-0 · Cited by 6

Integrin αIIbβ3

Bledzka, K. M., Pesho, M. M., Ma, Y., & Plow, E. F. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-387837-3.00012-2 · Cited by 6

Developmental expression of the fermitin/kindlin gene family in Xenopus laevis embryos

Canning, C. A., Chan, J. S. K., Common, J., Lane, E. B., & Jones, C. M. (2011) · Developmental Dynamics · doi:10.1002/dvdy.22683 · Cited by 6

The Kindlin protein family: new members to the club of focal adhesion proteins

Meves, A., Stremmel, C., Gottschalk, K. E., & Fässler, R. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.07.006 · Cited by 168

Kindlin Signaling and Bone

Cao, H., & Xiao, G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.11176-6

Kindlins in FERM adhesion

Malinin, N. L., Plow, E. F., & Byzova, T. V. (2010) · Blood · doi:10.1182/blood-2009-10-239269 · Cited by 129

Emerging evidence for kindlin oligomerization and its role in regulating kindlin function

Bu, W., Levitskaya, Z., Tan, S., & Gao, Y. (2021) · Journal of Cell Science · doi:10.1242/jcs.256115 · Cited by 30

How ILK and kindlins cooperate to orchestrate integrin signaling

Böttcher, R. T., Lange, A., & Fässler, R. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.05.008 · Cited by 48