Research progress of biological function in integrin-interacting protein kindlin family

doi:10.3969/j.issn.0529-1356.2014.05.024

Abstract

Abstract:

Integrin-interacting protein kindlin is a novel family of focal adhesion proteins consisting of three members, Kindlin-1, Kindlin-2 and Kindlin-3. Kindlins are highly conserved and belong to FERM-containing proteins. Present studies have showed there is a close relationship between Kindlin family and integrin activation and genetic diseases. In addition, Kindlin family is also a critical mediator for tumorigenesis. We review structural features, distribution and progress of biological functions of kindlin family in this paper.

Key words: Kindlin family, Integrin, Biological function

YANG Mei CHEN Xi ZHANG Shui-wen ZHANG Hong-quan*. Research progress of biological function in integrin-interacting protein kindlin family[J]. AAS, 2014, 45(6): 865-869.

References

［1］Lai-Cheong JE, Parsons M, McGrath JA. The role of kindlins in cell biology and relevance to human disease［J］. Int J Biochem Cell Biol, 2010, 42(5):595-603.
［2］Xu Z, Gao J, Hong J, et al. Integrity of kindlin-2 FERM subdomains is required for supporting integrin activation［J］. Biochem Biophys Res Commun, 2013, 434(2):382-387.
［3］Moser M, Legate KR, Zent R, et al. The tail of integrins, talin, and kindlins［J］. Science, 2009, 324(5929):895-899.
［4］Meves A, Stremmel C, Gottschalk K, et al. The Kindlin protein family: new members to the club of focal adhesion proteins［J］. Trends Cell Biol, 2009, 19(10):504-513.
［5］Larjava H, Plow EF, Wu C. Kindlins: essential regulators of integrin signalling and cell-matrix adhesion［J］. EMBO Rep, 2008, 9(12): 1203-1208.
［6］Siegel DH, Ashton GH, Penagos HG, et al. Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome［J］. Am J Hum Genet, 2003, 73(1):174-187.
［7］Ussar S, Wang HV, Linder S, et al. The Kindlins: subcellular localization and expression during murine development［J］. Exp Cell Res, 2006, 312(16):3142-3151.
［8］Plow EF, Qin J, Byzova T. Kindling the flame of integrin activation and function with kindlins［J］. Curr Opin Hematol, 2009, 16(5):323-328.
［9］Weinstein EJ, Bourner M, Head R, et al. URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas［J］. Biochim Biophys Acta, 2003, 1637(3):207-216.
［10］Zhao T, Guan L, Yu Y, et al. Kindlin-2 promotes genome instability in breast cancer cells［J］. Cancer Lett, 2013, 330(2):208-216.
［11］An Z, Dobra K, Lock JG, et al. Kindlin-2 is expressed in malignant mesothelioma and is required for tumor cell adhesion and migration［J］. Int J Cancer, 2010, 127(9):1999-2008.
［12］Harburger DS, Calderwood DA. Integrin signalling at a glance［J］. J Cell Sci, 2009, 122(Pt 2):159-163.
［13］Margadant C, Kreft M, Zambruno G, et al. Kindlin-1 regulates integrin dynamics and adhesion turnover［J］. PLoS One, 2013, 8(6):e65341.
［14］Montanez E, Ussar S, Schifferer M, et al. Kindlin-2 controls bidirectional signaling of integrins［J］. Genes Dev, 2008, 22(10):1325-1330.
［15］Moretti FA, Moser M, Lyck R, et al. Kindlin-3 regulates integrin activation and adhesion reinforcement of effector T cells［J］. Proc Natl Acad Sci USA, 2013, 110(42):17005-17010.
［16］Hart R, Stanley P, Chakravarty P, et al. The kindlin 3 pleckstrin homology domain has an essential role in lymphocyte function-associated antigen 1 (LFA-1) integrin-mediated B cell adhesion and migration［J］. J Biol Chem, 2013, 288(21):14852-14862.
［17］Moser M, Nieswandt B, Ussar S, et al. Kindlin-3 is essential for integrin activation and platelet aggregation［J］. Nat Med, 2008, 14(3):325-330.
［18］Ye F, Snider AK, Ginsberg MH. Talin and kindlin: the one-two punch in integrin activation［J］. Front Med, 2014, 8(1):6-16.
［19］Brahme NN, Harburger DS, Kemp-O’Brien K, et al. Kindlin binds migfilin tandem LIM domains and regulates migfilin focal adhesion localization and recruitment dynamics［J］. J Biol Chem, 2013, 288(49):35604-35616.
［20］Calderwood DA, Campbell ID, Critchley DR. Talins and kindlins: partners in integrin-mediated adhesion［J］. Nat Rev Mol Cell Biol, 2013, 14(8):503-517.
［21］Kindler T. Congenital poikiloderma with traumatic bulla formation and progressive cutaneous atrophy［J］. Br J Dermatol, 1954, 66(32):104-111.
［22］Ussar S, Moser M, Widmaier M, et al. Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction［J］. PLoS Genet, 2008, 4(12): e1000289.
［23］Sadler E, Klausegger A, Muss W, et al. Novel KIND1 gene mutation in Kindler syndrome with severe gastrointestinal tract involvement［J］. Arch Dermatol, 2006, 142(12): 1619-1624.
［24］Zhan J, Zhu X, Guo Y, et al. Opposite role of Kindlin-1 and Kindlin-2 in lung cancers［J］. PLoS One, 2012, 7(11):e50313.
［25］Mahawithitwong P, Ohuchida K, Ikenaga N, et al. Kindlin-1 expression is involved in migration and invasion of pancreatic cancer［J］. Int J Oncol, 2013, 42(4):1360-1366.
［26］Sin S, Bonin F, Petit V, et al. Role of the focal adhesion protein kindlin-1 in breast cancer growth and lung metastasis［J］. J Natl Cancer Inst, 2011, 103(17):1323-1337.
［27］Dowling JJ, Gibbs E, Russell M, et al. Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function［J］. Circ Res, 2008, 102(4):423-431.
［28］Hatcher CJ, Basson CT. Disrupted intercalated discs. Is kindlin-2 required［J］. Circ Res, 2008, 102(4):392-394.
［29］Pluskota E, Dowling JJ, Gordon, N, et al. The integrin coactivator kindlin-2 plays a critical role in angiogenesis in mice and zebrafish［J］. Blood, 2011, 117(18):4978-4987.
［30］Shen Z, Ye Y, Dong L, et al. Kindlin-2: a novel adhesion protein related to tumor invasion, lymph node metastasis, and patient outcome in gastric cancer［J］. Am J Surg, 2012, 203(2):222-229.
［31］Yu Y, Wu J, Guan L, et al, Kindlin 2 promotes breast cancer invasion via epigenetic silencing of the microRNA200 gene family［J］. Int J Cancer, 2013, 133(6):1368-1379.
［32］Gong X, An Z, Wang Y, et al. Kindlin-2 controls sensitivity of prostate cancer cells to cisplatin-induced cell death［J］. Cancer Lett, 2010, 299(1):54-62.
［33］Gozgit JM, Pentecost BT, Marconi SA, et al. Use of an aggressive MCF-7 cell line variant, TMX2-28, to study cell invasion in breast cancer［J］. Mol Cancer Res, 2006, 4(12):905-913.
［34］Yu Y, Wu J, Wang Y, et al. Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling［J］. EMBO Rep, 2012, 13(8):750-758.
［35］KasirerFriede A, Kang J, Kahner B, et al. ADAP interactions with talin and kindlin promote platelet integrin αIIbβ3 activation and stable fibrinogen binding［J］. Blood, 2014,123(20):3165-3166. 
［36］Svensson L, Howarth K, McDowall A, et al. Leukocyte adhesion deficiency-Ⅲ is caused by mutations in KINDLIN3 affecting integrin activation［J］. Nat Med, 2009, 15(3):306-312.
［37］Malinin NL, Zhang L, Choi J, et al. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans［J］. Nat Med, 2009, 15(3):313-318.
［38］Sossey-Alaoui K, Pluskota E, Davuluri G, et al. Kindlin-3 enhances breast cancer progression and metastasis by activating Twist-mediated angiogenesis［J］. FASEB J, 2014,28(5):2260-2271.
［39］Yang M, Du J, Lu D, et al. Increased expression of kindlin 2 in luteinized granulosa cells correlates with androgen receptor level in patients with polycystic ovary syndrome having hyperandrogenemia［J］. Reprod Sci, 2014, 21(6):696-703.
［40］Gao J, Khan AA, Shimokawa T, et al. A feedback regulation between Kindlin-2 and GLI1 in prostate cancer cells［J］. FEBS Lett, 2013, 587(6):631-638.

[1]	GUO Jian-lin WANG Xue-qing XU Cun-shuan. Advances in biological functions of miR-429 [J]. Acta Anatomica Sinica, 2022, 53(2): 266-272.
[2]	MA Dong-xue GAO Wei-juan HE Xiao-ping XU Li-jun LIU Ya-lei DONG Xian-hui. Effect of Astragalus, Epimedium and Pueraria compound on Alzheimer’s disease mice behaviors and hippocampus disintegrin and metalloprotease 10 expression#br# [J]. Acta Anatomica Sinica, 2020, 51(6): 821-826.
[3]	WANG Qi-wen LI Pan WANG Song-yun GUO Xue-qiang ZHANG Chun-yan YANG Ya-jun LI Jian-yong XU Cun-shuan. Circular RNA and its role in liver diseases [J]. Acta Anatomica Sinica, 2019, 50(5): 690-697.
[4]	MU Ling-min WANG Wen-feng GUO ZHi-kun* ZHANG Guang-mou. Expression of integrin CD11a, CD11b and CD11c during the rat heart development [J]. AAS, 2013, 44(4 ): 525-529.
[5]	. p38 promotes the expression of extracellular matrix induced by nicotine in vascular smooth muscle cells of rats BR>BR> [J]. , 2012, 43(1): 42-46.
[6]	. Effects of integrin-β1 during the process of laminin promoting Schwann cells to synthesis extracellular matrix [J]. , 2011, 42(4): 465-469.
[7]	. Effect of RGD stimulating integrin of cardiomyocyteson the uptake of macromolecules [J]. , 2010, 41(03): 473-476.